From owner-proteins@net.bio.net Tue Jun 01 01:43:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!dispose.news.demon.net!demon!newsfeed.nacamar.de!newsfeed.nacamar.de!fu-berlin.de!server1.netnews.ja.net!pegasus.csx.cam.ac.uk!hgmp.mrc.ac.uk!not-for-mail From: Maria Jesus Martin Newsgroups: bionet.molbio.proteins Subject: Release 10 of TrEMBL, a protein sequence database supplementing SWISS-PROT Date: Tue, 01 Jun 1999 10:36:54 +0100 Organization: EMBL-EBI Message-ID: <3753A9B6.6461C3CF@ebi.ac.uk> Reply-To: martin@ebi.ac.uk NNTP-Posting-Host: burns.ebi.ac.uk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: niobium.hgmp.mrc.ac.uk 928229815 27667 193.62.196.82 (1 Jun 1999 09:36:55 GMT) X-Complaints-To: news@hgmp.mrc.ac.uk NNTP-Posting-Date: 1 Jun 1999 09:36:55 GMT X-Mailer: Mozilla 4.06 [en] (X11; U; Linux 2.0.36 i686) Lines: 96 INTRODUCTION ============ TrEMBL is a protein sequence database supplementing the SWISS-PROT Protein Sequence Data Bank. TrEMBL contains the translations of all coding sequences (CDS) present in the EMBL Nucleotide Sequence Database not yet integrated in SWISS-PROT. TrEMBL can be considered as a preliminary section of SWISS-PROT. For all TrEMBL entries which should finally be upgraded to the standard SWISS-PROT quality, SWISS-PROT accession numbers have been assigned. RELEASE 10.0 OF TrEMBL ===================== This TrEMBL release is created from the EMBL Nucleotide Sequence Database release 58 and contains 244'862 sequence entries, comprising 66'562'800 amino acids. TrEMBL is split in two main sections; SP-TrEMBL and REM-TrEMBL: SP-TrEMBL (SWISS-PROT TrEMBL) contains the entries (201'082), which should be eventually incorporated into SWISS-PROT. SWISS-PROT accession numbers have been assigned for all SP-TrEMBL entries. SP-TrEMBL is organized in subsections: arc.dat (Archea): 7408 entries fun.dat (Fungi): 6679 entries hum.dat (Human): 8518 entries inv.dat (Invertebrates): 23653 entries mam.dat (Other Mammals): 3130 entries mhc.dat (MHC proteins): 4236 entries org.dat (Organelles): 16261 entries phg.dat (Bacteriophages): 1971 entries pln.dat (Plants): 17352 entries pro.dat (Prokaryotes): 45992 entries rod.dat (Rodents): 7480 entries unc.dat (Unclassified): 44 entries vrl.dat (Viruses): 53916 entries vrt.dat (Other Vertebrates): 4442 entries REM-TrEMBL (REMaining TrEMBL) contains the entries (46'785) that we do not want to include in SWISS-PROT. WEEKLY UPDATES OF TrEMBL AND NON-REDUNDANT DATA SETS ==================================================== Weekly cumulative updates of TrEMBL are available by anonymous FTP and from the EBI SRS server. We also produce every week a complete non-redundant protein sequence collection by providing three compressed files (these are in the directory /pub/databases/sp_tr_nrdb on the EBI FTP server): sprot.dat.Z, trembl.dat.Z and trembl_new.dat.Z. ACCESS/DATA DISTRIBUTION ======================== FTP server: ftp.ebi.ac.uk/pub/databases/trembl SRS server: http://srs.ebi.ac.uk/ TREMBL is also available on the SWISS-PROT CD-ROM. SWISS-PROT + TREMBL is searchable on the FASTA3, BLAST2 and Bic_sw servers of the EBI. TrEMBL HAS BEEN PREPARED BY: ============================ Rolf Apweiler, Kirsty Bates, Margaret Biswas, Sergio Contrino, Wolfgang Fleischmann, Gill Fraser, Henning Hermjakob, Vivien Junker, Youla Karavidopoulou, Fiona Lang, Minna Lehvaslaiho, Michele Magrane, Maria Jesus Martin, Steffen Moeller, Nicoletta Mitaritonna, Nicola Mulder, Claire O'Donovan and Eleanor Whitfield at the EMBL Outstation - European Bioinformatics Institute (EBI) in Hinxton, UK; Amos Bairoch and Alain Gateau at the Swiss Institute of Bioinformatics in Geneva, Switzerland. ----------------------------------------------------------------- Maria Jesus Martin email:martin@ebi.ac.uk EMBL Outstation EBI (European Bioinformatics Institute) URL: http://www.ebi.ac.uk Wellcome Trust Genome Campus Tel: +44 (1223) 494408 Hinxton fax: +44 (1223) 494468 Cambridge CB10 1SD UK ----------------------------------------------------------------- From owner-proteins@net.bio.net Tue Jun 01 07:13:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!newsfeed.nacamar.de!newsfeed.nacamar.de!news-fra.pop.de!newsfeed.ecrc.net!news.belnet.be!news.rediris.es!news.uv.es!not-for-mail From: paz Newsgroups: bionet.molbio.proteins Subject: metalloproteinases Date: Tue, 01 Jun 1999 17:03:50 +0200 Organization: Universitat de Valencia Message-ID: <3753F655.FACF9227@ibv.csic.es> NNTP-Posting-Host: 193.146.183.148 Mime-Version: 1.0 Content-Type: text/plain; charset=iso-8859-1 Content-Transfer-Encoding: 8bit X-Trace: peque.uv.es 928249439 22592 193.146.183.148 (1 Jun 1999 15:03:59 GMT) X-Complaints-To: postmaster@uv.es NNTP-Posting-Date: 1 Jun 1999 15:03:59 GMT X-Mailer: Mozilla 4.6 [en] (Win98; I) X-Accept-Language: en Lines: 4 I am a student, and i am studing a particalars proteins, the metalloproteinases. I don´t know about of that. If somebody know about of that i would be very grateful. From owner-proteins@net.bio.net Wed Jun 02 08:04:00 1999 Path: biosci!NS.GLC.CN.NET!longjy From: longjy@NS.GLC.CN.NET (Jianyin Long) Newsgroups: bionet.molbio.proteins Subject: vefg Date: 2 Jun 1999 09:04:17 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 7 Sender: daemon@net.bio.net Distribution: world Message-ID: <37555471.35340659@ns.glc.cn.net> Reply-To: longjy@cheerful.com NNTP-Posting-Host: net.bio.net I'm wondering that if fusion of some short peptides to the c-terminal of VEGF has any effects on the expression of VEGF and its bioactivity ? v From owner-proteins@net.bio.net Wed Jun 02 08:57:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!newsfeed.berkeley.edu!skynet.be!poster!not-for-mail From: "Fiers-Vercruysse" Newsgroups: bionet.molbio.proteins Subject: plant biotechnology club Date: Wed, 2 Jun 1999 18:50:58 +0200 Organization: Belgacom Skynet SA/NV Lines: 41 Message-ID: <7j3nf9$rvk$1@news1.skynet.be> NNTP-Posting-Host: dialup23.mechelen.skynet.be X-Trace: news1.skynet.be 928342313 28660 195.238.30.23 (2 Jun 1999 16:51:53 GMT) X-Complaints-To: abuse@skynet.be NNTP-Posting-Date: 2 Jun 1999 16:51:53 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2014.211 Dear all, this is a message in which i will present a new online club for people interested in plant molecular biology. It does not contain any question or answer to a problem mentioned higher. Please ignore if not interested. The plant biotechnology club is a club recently founded to bring together researchers in the field of plant molecular biology from all over the world to discuss the research in there area. With the controverse existing these days about GMOs in the media our discussions have been concentrating on that topic: the ethic aspects of genetic engineering of plants, public opinion, environmental aspects, etc. But it is also the goal of the club to discuss research problems and advances. Currently there are two founders in this club: Shai Lawit, graduate student in plant molecular biology at the University of Florida and Dan Hancock, medical student at Cambridge. They 'lead' the discussions and bring up new topics to discuss in order to keep the quality of the discussions as high as possible. The club mostly works via its message board where every member can post a message that all other members can read and reply to at later times (just as in newsgroups). In addition to this there is also a place where links can be added to interesting sites on the internet concerning the subject. (A very interesting link that has been added there is to the yahoo full coverage site on the news about GMOs where you can follow up the most recent news on the subject.) Also a place in this club that may be of much interest in the future is the chat room to discuss topics in a more direct way. This club has been started up 3 weeks ago and I guess it will need some time to grow bigger to become as interesting as it is intended to be. That is why we keep on looking for interesting and interested members to participate in our club. The more people, the more ideas! Nevertheless, we have had already some interesting discussions. You can find the club at http://clubs.yahoo.com/clubs/plantbiotechnology. If you want to obtain more information about how to funtion in the club, mail your questions to gentech2002@yahoo.com. From owner-proteins@net.bio.net Wed Jun 02 14:45:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!chippy.visi.com!hermes.visi.com!news-out.visi.com!news.maxwell.syr.edu!newsfeed.cwix.com!128.174.5.49!vixen.cso.uiuc.edu!not-for-mail From: colby Newsgroups: bionet.molbio.proteins Subject: H-bonding side-chains Date: Wed, 02 Jun 1999 17:44:00 -0500 Organization: University of Illinois at Urbana-Champaign Lines: 13 Message-ID: <3755B3B0.8B801D00@uiuc.edu> NNTP-Posting-Host: bambam.scs.uiuc.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.51 [en] (WinNT; U) X-Accept-Language: en Can the side chain of a tryptophan residue accept a H-bond? What about an arginine residue? According to http://swift.embl-heidelberg.de/future/aainfo/hbonds.html, the only site on the web I found that discusses amino acid side chain H-bonding, these two residues do not seem to accept H-bonds. Is it because of steric hindrance by the atoms that the N-atoms are bonded to? If so, why does it not affect the H-bond accepting capability of histidine? I appreciate any replies. From owner-proteins@net.bio.net Wed Jun 02 17:55:00 1999 Path: biosci!newshost.lanl.gov!awabi.library.ucla.edu!128.230.129.106!news.maxwell.syr.edu!sunqbc.risq.qc.ca!carnaval.risq.qc.ca.POSTED!not-for-mail From: "Benoit Pelletier" Newsgroups: bionet.molbio.proteins Subject: alcohol dehydrogenase MW Lines: 4 X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2014.211 Message-ID: Date: Thu, 03 Jun 1999 01:50:04 GMT NNTP-Posting-Host: 206.167.181.108 X-Trace: carnaval.risq.qc.ca 928374604 206.167.181.108 (Wed, 02 Jun 1999 21:50:04 EDT) NNTP-Posting-Date: Wed, 02 Jun 1999 21:50:04 EDT Can some one give me molecular weight of alcohol dehydrogenase enzyme ??? From owner-proteins@net.bio.net Wed Jun 02 21:52:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!dispose.news.demon.net!demon!news.maxwell.syr.edu!news-peer.gip.net!news.gsl.net!gip.net!portc01.blue.aol.com!audrey01.news.aol.com!not-for-mail From: baron0805@aol.com (Baron0805) Newsgroups: bionet.molbio.proteins Subject: Re: H-bonding side-chains NNTP-Posting-Host: ladder05.news.aol.com X-Admin: news@aol.com Date: 3 Jun 1999 05:46:50 GMT Organization: AOL http://www.aol.com References: <3755B3B0.8B801D00@uiuc.edu> Message-ID: <19990603014650.10959.00000349@ng-fd1.aol.com> Lines: 8 I looked in my Cell book to see what you were talking about. Both of these structures are very stable structures. Tryptphan is stabilized by the ring structures and Arginine is stabilized by its resonance ability. I would say that these two amino acids are able to H-bond, but it is very unlikely due to resonance. That would be my guess. Junior, Biology, University of Southern Indiana Question everything!!!! From owner-proteins@net.bio.net Wed Jun 02 23:35:00 1999 Path: biosci!newshost.lanl.gov!arclight.uoregon.edu!wn4feed!worldnet.att.net!207.172.3.37!feed1.news.rcn.net!rcn!netnews.com!newspeer.monmouth.com!news-was.dfn.de!news-han1.dfn.de!news.gwdg.de!not-for-mail From: Steffen Schmidt Newsgroups: bionet.molbio.proteins Subject: pk of Threonin Date: Thu, 03 Jun 1999 07:49:30 +0200 Organization: GWDG, Goettingen Lines: 35 Message-ID: <3756176A.5E45B8EA@Uni-MolGen.gwdg.de> NNTP-Posting-Host: 134.76.70.65 Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------E26008AF265D99F74D268E6F" X-Mailer: Mozilla 4.5 [en] (WinNT; I) X-Accept-Language: en This is a multi-part message in MIME format. --------------E26008AF265D99F74D268E6F Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Hi, does anyone know the pk-value of the hydroxy-group of threonin, or a citation where I can find it. Thanks, Steffen --------------E26008AF265D99F74D268E6F Content-Type: text/x-vcard; charset=us-ascii; name="sschmid2.vcf" Content-Transfer-Encoding: 7bit Content-Description: Card for Steffen Schmidt Content-Disposition: attachment; filename="sschmid2.vcf" begin:vcard n:Schmidt;Steffen tel;work:Arbeitsgruppe PD Dr. R. Sterner x-mozilla-html:FALSE url:http://www.gwdg.de/~sschmid3 org:Institut für Mikrobiologie und Genetik;Abteilung für molekulare Genetik und präparative Molekularbiologie adr:;;Grisebachstr. 8;37077 Göttingen;;; version:2.1 email;internet:sschmid2@Uni-MolGen.gwdg.de title:Georg-August Universität Göttingen fn:Steffen Schmidt end:vcard --------------E26008AF265D99F74D268E6F-- From owner-proteins@net.bio.net Thu Jun 03 08:15:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!su-news-hub1.bbnplanet.com!washdc3-snf1!news.gtei.net!news.ums.edu!gamera.cbl.umces.edu!news.umces.edu!cbl.umces.edu!reno From: "Reno T. Nguyen" Newsgroups: bionet.molbio.proteins Subject: Re: H-bonding side-chains Date: Thu, 3 Jun 1999 12:00:28 -0400 Organization: University of Maryland Chesapeake Biological Laboratory Lines: 48 Message-ID: References: <3755B3B0.8B801D00@uiuc.edu> NNTP-Posting-Host: cbl.umces.edu Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII X-Trace: gamera.cbl.umces.edu 928425636 25104 131.118.224.6 (3 Jun 1999 16:00:36 GMT) X-Complaints-To: feedback@cbl.umces.edu NNTP-Posting-Date: 3 Jun 1999 16:00:36 GMT To: colby In-Reply-To: <3755B3B0.8B801D00@uiuc.edu> Hi, Check out the URL address http://www.proteometrics.com/aainfo/contents.htm There's info. on residue hydrogen bonding for Arginine and tryptophan. Reno Nguyen On Wed, 2 Jun 1999, colby wrote: > Date: Wed, 02 Jun 1999 17:44:00 -0500 > From: colby > Newsgroups: bionet.molbio.proteins > Subject: H-bonding side-chains > > Can the side chain of a tryptophan residue accept a H-bond? What about > an arginine residue? > > According to http://swift.embl-heidelberg.de/future/aainfo/hbonds.html, > the only site on the web I found that discusses amino acid side chain > H-bonding, these two residues do not seem to accept H-bonds. Is it > because of steric hindrance by the atoms that the N-atoms are bonded to? > If so, why does it not affect the H-bond accepting capability of > histidine? > > I appreciate any replies. > > > > ************************************************************************* Reno T. Nguyen Chesapeake Biological Laboratory /----\ /-----\ / Univ. MD Center for Environmental Science / / / / P.O. Box 38 / /______/ / Solomons, MD 20688 / / \ / / / // Tel: (410) 326-7261 \_______/ \_______/ \_______/ (410) 326-7409 Fax: (410) 326-7341 E-mail: reno@cbl.umces.edu ************************************************************************ From owner-proteins@net.bio.net Thu Jun 03 08:25:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!su-news-hub1.bbnplanet.com!washdc3-snf1!news.gtei.net!news.ums.edu!gamera.cbl.umces.edu!news.umces.edu!cbl.umces.edu!reno From: "Reno T. Nguyen" Newsgroups: bionet.molbio.proteins Subject: Re: pk of Threonin Date: Thu, 3 Jun 1999 12:19:52 -0400 Organization: University of Maryland Chesapeake Biological Laboratory Lines: 51 Message-ID: References: <3756176A.5E45B8EA@Uni-MolGen.gwdg.de> NNTP-Posting-Host: cbl.umces.edu Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII X-Trace: gamera.cbl.umces.edu 928426794 25356 131.118.224.6 (3 Jun 1999 16:19:54 GMT) X-Complaints-To: feedback@cbl.umces.edu NNTP-Posting-Date: 3 Jun 1999 16:19:54 GMT To: Steffen Schmidt In-Reply-To: <3756176A.5E45B8EA@Uni-MolGen.gwdg.de> Hi, Check out the URL address http://www.proteometrics.com/aainfo/contents.htm You'll find info on the pKa values for the side chains of amino acids that ionize. Threonine's hydroxy side chain does not ionize. You won't find any pKa value for Thr, other than for its alpha amino and carboxyl groups. Only the side chains of the following amino acids will ionize: Arg (guanido group) Asp (beta carboxylic acid) Cys (sulfhydryl) Glu (gamma carboxylic acid) His (imidazole) Lys (epsilon amino group) Tyr (phenol) Reno Nguyen On Thu, 3 Jun 1999, Steffen Schmidt wrote: > Date: Thu, 03 Jun 1999 07:49:30 +0200 > From: Steffen Schmidt > Newsgroups: bionet.molbio.proteins > Subject: pk of Threonin > > Hi, > > does anyone know the pk-value of the hydroxy-group of threonin, or a > citation where I can find it. > > Thanks, Steffen > ************************************************************************* Reno T. Nguyen Chesapeake Biological Laboratory /----\ /-----\ / Univ. MD Center for Environmental Science / / / / P.O. Box 38 / /______/ / Solomons, MD 20688 / / \ / / / // Tel: (410) 326-7261 \_______/ \_______/ \_______/ (410) 326-7409 Fax: (410) 326-7341 E-mail: reno@cbl.umces.edu ************************************************************************ From owner-proteins@net.bio.net Thu Jun 03 10:13:00 1999 Path: biosci!newshost.lanl.gov!arclight.uoregon.edu!hammer.uoregon.edu!vixen.cso.uiuc.edu!not-for-mail From: colby Newsgroups: bionet.molbio.proteins Subject: Re: H-bonding side-chains Date: Thu, 03 Jun 1999 13:07:44 -0500 Organization: None Lines: 15 Message-ID: <3756C470.41C6@uiuc.edu> References: <3755B3B0.8B801D00@uiuc.edu> <19990603014650.10959.00000349@ng-fd1.aol.com> NNTP-Posting-Host: leucine.ncsa.uiuc.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01 (X11; I; IRIX 5.3 IP12) Baron0805 wrote: > > I looked in my Cell book to see what you were talking about. Both of these > structures are very stable structures. Tryptphan is stabilized by the ring > structures and Arginine is stabilized by its resonance ability. I would say > that these two amino acids are able to H-bond, but it is very unlikely due to > resonance. That would be my guess. Thanks for your reply. It prompts me to ask why histidine is able to accept a H-bond - in fact both N-atoms in the His sidechain can be H-bond acceptors. Does histidine not have resonance stabilization too? (You can find details at http://swift.embl-heidelberg.de/future/aainfo/hbonds.html). -colby From owner-proteins@net.bio.net Thu Jun 03 10:20:00 1999 Path: biosci!newshost.lanl.gov!arclight.uoregon.edu!hammer.uoregon.edu!vixen.cso.uiuc.edu!not-for-mail From: colby Newsgroups: bionet.molbio.proteins Subject: Re: H-bonding side-chains Date: Thu, 03 Jun 1999 13:14:53 -0500 Organization: None Lines: 32 Message-ID: <3756C61D.167E@uiuc.edu> References: <3755B3B0.8B801D00@uiuc.edu> NNTP-Posting-Host: leucine.ncsa.uiuc.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01 (X11; I; IRIX 5.3 IP12) Reno T. Nguyen wrote: > > Hi, > > Check out the URL address http://www.proteometrics.com/aainfo/contents.htm > There's info. on residue hydrogen bonding for Arginine and tryptophan. Hi, Thanks for your reply. But the site you mention has the same link as the site I mentioned earlier, it was the data at this site that made me raise the question. I'm interested in knowing what makes the His side chain an *acceptor* of H-bonds, but not the Arg and Trp side chains. (All these side chains do act as H-bond *donors*). I appreciate any replies. -colby > On Wed, 2 Jun 1999, colby wrote: > > > Date: Wed, 02 Jun 1999 17:44:00 -0500 > > From: colby > > Newsgroups: bionet.molbio.proteins > > Subject: H-bonding side-chains > > > > Can the side chain of a tryptophan residue accept a H-bond? What about > > an arginine residue? > > > > According to http://swift.embl-heidelberg.de/future/aainfo/hbonds.html, > > the only site on the web I found that discusses amino acid side chain > > H-bonding, these two residues do not seem to accept H-bonds. From owner-proteins@net.bio.net Thu Jun 03 10:52:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!uchinews2!newsswitch.lcs.mit.edu!netnews.com!news-peer1.sprintlink.net!news-in-west1.sprintlink.net!news.sprintlink.net!news.aecom.yu.edu!fengli From: Tristan Newsgroups: sci.research.postdoc,bionet.molbio.proteins,bionet.general Subject: Re: Postdocs in biochemistry & molecular biology, U. of Chicago Date: Thu, 03 Jun 1999 14:41:32 -0400 Organization: Albert Einstein College of Medicine Lines: 31 Distribution: na Message-ID: <030619991441325243%fengli@aecom.yu.edu> References: NNTP-Posting-Host: skylark.aecom.yu.edu Mime-Version: 1.0 Content-Type: text/plain; charset=HZ-GB-2312 Content-Transfer-Encoding: 8bit To: jm68@midway.uchicago.edu (Jim Mensch) Posted-And-Mailed: yes User-Agent: YA-NewsWatcher/4.2.2 Xref: biosci bionet.molbio.proteins:14429 bionet.general:33208 [[ This message was both posted and mailed: see the "To," "Cc," and "Newsgroups" headers for details. ]] No email responses allowed and you will discard all emails? That's why you have to post your message twice on the newsgroup! Don't annoy other people anymore if you feel annoyed by other people's email. Tris In article , Jim Mensch wrote: > Two postdoctoral research positions will soon be available at the Kennedy > Mental Retardation and Connective Tissue Research Center located at the > University of Chicago, Chicago IL. These positions will involve research > projects in the areas of protein biochemistry/enzymology and molecular > biology. To be considered for these appointments, and for further > information, please write to: > > Postdoctoral Search > Kennedy Center, MC5058 > 5841 S. Maryland Ave. > Chicago IL 60637 > > Please include curriculum vitae in your correspondence. No phone calls or > email please. The person posting this announcement is not reviewing the > applicants; all email responses will be discarded. > ^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^^ From owner-proteins@net.bio.net Thu Jun 03 11:03:00 1999 Newsgroups: bionet.molbio.proteins Subject: Re: pk of Threonin From: immune@intergate.bc.ca (immunechem) Reply-To: immune@intergate.bc.ca Organization: Internet Gateway X-Newsreader: WinVN 0.99.7 References: <3756176A.5E45B8EA@Uni-MolGen.gwdg.de> MIME-Version: 1.0 Content-Type: Text/Plain; charset=US-ASCII NNTP-Posting-Host: pm45s14.intergate.bc.ca Message-ID: <3756cefa@carrera.intergate.ca> Date: 3 Jun 1999 11:52:42 -0800 X-Trace: 3 Jun 1999 11:52:42 -0800, pm45s14.intergate.bc.ca Lines: 64 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!newsfeed.direct.ca!news.vphos.net!carrera.intergate.ca!pm45s14.intergate.bc.ca even at pH 14? I though any OH group is analog of water. then should be ionizable In article , reno@cbl.umces.edu says... > > >Hi, > >Check out the URL address http://www.proteometrics.com/aainfo/contents.htm >You'll find info on the pKa values for the side chains of amino acids that >ionize. Threonine's hydroxy side chain does not ionize. You won't find >any pKa value for Thr, other than for its alpha amino and carboxyl groups. >Only the side chains of the following amino acids will ionize: > >Arg (guanido group) >Asp (beta carboxylic acid) >Cys (sulfhydryl) >Glu (gamma carboxylic acid) >His (imidazole) >Lys (epsilon amino group) >Tyr (phenol) > > >Reno Nguyen > > >On Thu, 3 Jun 1999, Steffen Schmidt wrote: > >> Date: Thu, 03 Jun 1999 07:49:30 +0200 >> From: Steffen Schmidt >> Newsgroups: bionet.molbio.proteins >> Subject: pk of Threonin >> >> Hi, >> >> does anyone know the pk-value of the hydroxy-group of threonin, or a >> citation where I can find it. >> >> Thanks, Steffen >> > > >*********************************************************************** ** >Reno T. Nguyen >Chesapeake Biological Laboratory /----\ /-----\ / >Univ. MD Center for Environmental Science / / / / >P.O. Box 38 / /______/ / >Solomons, MD 20688 / / \ / > / / // >Tel: (410) 326-7261 \_______/ \_______/ \_______/ > (410) 326-7409 >Fax: (410) 326-7341 >E-mail: reno@cbl.umces.edu >*********************************************************************** * > > From owner-proteins@net.bio.net Thu Jun 03 11:51:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!newsswitch.lcs.mit.edu!newsfeed.cwix.com!192.195.196.233!testbox!not-for-mail Message-ID: <3756DB98.5937@bridgew.edu> From: "Frank R. Gorga" Reply-To: fgorga@bridgew.edu Organization: Bridgewater State College X-Mailer: Mozilla 3.0 (Win95; I) MIME-Version: 1.0 Newsgroups: bionet.molbio.proteins Subject: Re: H-bonding side-chains References: <3755B3B0.8B801D00@uiuc.edu> Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Lines: 64 Date: Thu, 03 Jun 1999 15:46:32 -0400 NNTP-Posting-Host: 134.241.191.50 X-Trace: testbox 928439125 134.241.191.50 (Thu, 03 Jun 1999 15:45:25 EDT) NNTP-Posting-Date: Thu, 03 Jun 1999 15:45:25 EDT colby wrote: > > Can the side chain of a tryptophan residue accept a H-bond? What about > an arginine residue? > > According to http://swift.embl-heidelberg.de/future/aainfo/hbonds.html, > the only site on the web I found that discusses amino acid side chain > H-bonding, these two residues do not seem to accept H-bonds. Is it > because of steric hindrance by the atoms that the N-atoms are bonded to? > If so, why does it not affect the H-bond accepting capability of > histidine? > > I appreciate any replies. The simple answer is "yes"... the side chains of all of these residues (Tyr, Arg & His) are chemically capable of both donating to and accepting hydrogen bonds. Wether they will do so in a specific situtation in a protein is, of course, much more complicated. Here is the longer answer... Hydrogen bonding requirements Donor -- a polar X-H bond i.e. X is significantly more electronegative than H; for proteins X is almost always N or O Acceptor -- -Y: i.e. an electronegative atom with a nonbonded (lone) pair of electrons, again for proteins this is almost always N or O Bottom line -- The hydroxyl (OH) of tyrosine is capable of both donating to and accepting H bonds The same is true for both the guanidium group of arg and the imidazole group of histidine. As for resonance (suggested in other replies)... it has nothing to do with hydrogen bonding. Biochemically -- The situtation in proteins is much more complicated... in order to form a H-bond in proteins both donor and acceptor have to be positioned properly with respect to one another (both angle and distance are critical). The polarity of environment is also critical... the more polar the enviroment the less likely a residue will be H-boned to anything other that water. Hope this helps, -- FRG ********************************* Frank R. Gorga, Ph.D. Department of Chemical Sciences Bridgewater State College Bridgewater, MA 02325 (508) 697-1200 x2827 fgorga@bridgew.edu From owner-proteins@net.bio.net Thu Jun 03 13:47:00 1999 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!dispose.news.demon.net!demon!newsfeed.tli.de!grolier!club-internet!not-for-mail From: "ciavatti" Newsgroups: bionet.molbio.proteins Subject: nitrosomonas Date: Thu, 3 Jun 1999 23:39:17 +0200 Organization: Club-Internet (France) Message-ID: <7j6sp0$t21$1@front3.grolier.fr> NNTP-Posting-Host: lorient-1-1.club-internet.fr X-Trace: front3.grolier.fr 928446048 29761 195.36.142.1 (3 Jun 1999 21:40:48 GMT) NNTP-Posting-Date: 3 Jun 1999 21:40:48 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2014.211 Lines: 14 I search informations on oxydation of NH4+ by Nitosomonas : all pot Redox of electron transporteurs synthesis of ATP? What is the hydogen and electron accepteur? how does Nitrosomonas incorporate CO2? and also the same informations for chiomiotrophic bacteria using H2S with many thanks G. Ciavatti ciavatti@club-internet.fr http://perso.club-internet.fr/ciavatti/evolution/evolution.htm From owner-proteins@net.bio.net Thu Jun 03 15:08:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!awabi.library.ucla.edu!164.67.43.25!news.ucla.edu!not-for-mail From: "Kevin Klapstein" Newsgroups: bionet.molbio.proteins Subject: Request for help regarding homology recognition by RecA Date: 3 Jun 1999 23:02:44 GMT Organization: University of California, Los Angeles Lines: 24 Message-ID: <01beae13$53a3adc0$1c9c8e95@gradlab_pc_2.biomath.medsch.ucla.edu> NNTP-Posting-Host: 149.142.156.28 X-Newsreader: Microsoft Internet News 4.70.1155 Hello; I'm currently studying RecA, and I'm interested in the homology recognition part of the strand exchange process. Particularly puzzling to us right now is how homology is recognized between two DNA molecules when one of them (the one bound to RecA) is extended by 50%. There are also some topological problem I am trying to work out that seem very stubborn. If anybody reading this has an interest in or knowledge about the homology recognition phase of RecA facilitated strand exchange and wouldn't mind talking to a confused graduate student for a little while, please drop me a line. Cheers, Kevin kklap@biomath.medsch.ucla.edu From owner-proteins@net.bio.net Mon Jun 07 03:55:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!news-feed.inet.tele.dk!bofh.vszbr.cz!news.daimi.au.dk!not-for-mail From: "Ditlev Brodersen" Newsgroups: bionet.molbio.proteins Subject: XAct: A program for construction of crystallisation trials Date: Mon, 7 Jun 1999 13:40:15 +0200 Organization: IMSB, Aarhus University, Denmark Lines: 60 Message-ID: <7jgb46$4396o$1@xinwen.daimi.au.dk> Reply-To: "Ditlev Brodersen" NNTP-Posting-Host: dings.imsb.au.dk X-Trace: xinwen.daimi.au.dk 928755654 4302040 255.255.255.255 (7 Jun 1999 11:40:54 GMT) X-Complaints-To: news@daimi.au.dk NNTP-Posting-Date: 7 Jun 1999 11:40:54 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2014.211 SOFTWARE ANNOUNCEMENT: ***************************************************************** XAct 1.0 for Windows 95/98 A Program for Contruction, Automated Setup, and Bookkeeping of Crystallisation Experiments Macromolecular Crystallography Institute of Molecular and Structural Biology Aarhus University Denmark ***************************************************************** XAct is a stand-alone application for Microsoft Windows 95/98 that can be used to construct, maintain, and record the results of many crystallisation experiments. Through an extensive object-oriented data structure, the program supports multiple users each with many crystallisation experiments organised in a hierarchical fashion. The program has been developed in the Laboratory for Macromolecular Crystallography, Institute of Molecular and Structural Biology, Aar- hus University, Denmark headed by Asc. Prof. Jens Nyborg. XAct is being used on a daily basis in our laboratory by technicians, students, grad. students, and post.doc.'s to set up crystalisation trials in an organised way. At the moment, the program can be down- loaded in a late beta-version. The software is available free of change to all academic users after the registration form has been completed. Registration and download is done through the XAct homepage at http://zombie.imsb.au.dk/xact This page also contains additional information about the software, screen shots, manual, references, etc. The program supports automatic dispensing of the designed solutions using a Gilson model 222 autosampler attached to the PC. We are espe- cially interested in response from people who have this equipment in the lab and who might wish to use it for setting up crystallisation trials. Ditlev Brodersen -=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=-=- __ /_/\ Ditlev E. Brodersen Phone: +45 8942 5021 / /\ \ M.Sc., Ph.D. student Fax : +45 8620 1222 / / /\ \ IMSB, Aarhus University Email: ding@imsb.au.dk / / /\ \ \ Gustav Wieds Vej 10c WWW : http://imsb.au.dk/~ding/ / /_/__\ \ \ DK-8000 Aarhus C /_/______\_\/\ Denmark \_\_________\/ From owner-proteins@net.bio.net Mon Jun 07 17:30:00 1999 Path: biosci!esr.cri.nz!Rachael.Russell From: Rachael.Russell@esr.cri.nz ("Russell, Rachael") Newsgroups: bionet.molbio.proteins Subject: Cell lysing for protein assay Date: 7 Jun 1999 18:30:27 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 12 Sender: daemon@net.bio.net Distribution: world Message-ID: <9173148B8F8CD1118AAC00805F0649C66C2C61@KSCXCHG2> NNTP-Posting-Host: net.bio.net Hi there I am looking for protocols cell lysing for Luciferase assays - I have a kit that has everything but the lysing buffer! If anyone has any ideas, please let me know. Am currently using an EDTA/PBS/Triton X-100 buffer, but would like to know of more possibile buffers, and methods ie how long to incubate buffer. (I am using adherant cells in 96-well plates) Thanks Rachael Russell ESR Kenepuru Science Centre New Zealand From owner-proteins@net.bio.net Tue Jun 08 14:24:00 1999 From: "Tom Johnston" Newsgroups: bionet.molbio.proteins Subject: horseradish peroxidase Date: Tue, 8 Jun 1999 23:09:43 +0100 Lines: 8 X-Newsreader: Microsoft Outlook Express 4.72.3110.1 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.3110.3 NNTP-Posting-Host: 194.131.244.249 Message-ID: <375d949a@news.jakinternet.co.uk> X-Trace: 8 Jun 1999 23:09:30 GMT, 194.131.244.249 Path: biosci!newshost.lanl.gov!logbridge.uoregon.edu!news.maxwell.syr.edu!tank.news.pipex.net!pipex!peernews!news.jakinternet.co.uk!194.131.244.249 Does anyone know if horseradish peroxidase has sialic acids on its carbohydrates and if so what type(s)? Cheers, Tom From owner-proteins@net.bio.net Wed Jun 09 09:27:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!arclight.uoregon.edu!wn4feed!worldnet.att.net!wnmaster2!not-for-mail From: "Bob" Newsgroups: bionet.molbio.proteins Subject: how to calculate the molar absorption coefficient of a protein? Date: Wed, 9 Jun 1999 13:21:37 -0400 Organization: AT&T WorldNet Services Lines: 11 Message-ID: <7jm7qv$ing$1@bgtnsc02.worldnet.att.net> NNTP-Posting-Host: 12.78.211.42 X-Trace: bgtnsc02.worldnet.att.net 928948895 19184 12.78.211.42 (9 Jun 1999 17:21:35 GMT) X-Complaints-To: abuse@worldnet.att.net NNTP-Posting-Date: 9 Jun 1999 17:21:35 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2014.211 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2014.211 Is there any web site that would calculate the absorption coefficient of a protein on the basis of the number of tryptophans, tyrosins, Phe, disulfide bonds... Or if not, what is the formula? Thanks, Rob From owner-proteins@net.bio.net Wed Jun 09 10:51:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!europa.netcrusader.net!206.228.179.2!news-peer1.sprintlink.net!news-in-central.sprintlink.net!news.sprintlink.net!news.aecom.yu.edu!not-for-mail From: gottfrie@aecom.yu.edu (David Gottfried) Newsgroups: bionet.molbio.proteins Subject: Re: how to calculate the molar absorption coefficient of a protein? Date: 9 Jun 1999 18:41:01 GMT Organization: AECOM Bronx, NY Lines: 16 Message-ID: <7jmcft$a4q$1@moonbeam.aecom.yu.edu> References: <7jm7qv$ing$1@bgtnsc02.worldnet.att.net> Reply-To: gottfrie@aecom.yu.edu (David Gottfried) NNTP-Posting-Host: photon.aecom.yu.edu Mime-Version: 1.0 Content-Type: text/plain; charset=US-ASCII Content-Transfer-Encoding: 7bit X-Newsreader: IBM NewsReader/2 2.0 In <7jm7qv$ing$1@bgtnsc02.worldnet.att.net>, "Bob" writes: >Is there any web site that would calculate the absorption coefficient of a >protein on the basis of the number of tryptophans, tyrosins, Phe, disulfide >bonds... > >Or if not, what is the formula? > See the article: Gill and von Hippel, Analytical Biochemistry 182, 319-326 (1989). ---------------------------- David S. Gottfried, Ph.D. Dept. of Physiology and Biophysics Albert Einstein College of Medicine ---------------------------- From owner-proteins@net.bio.net Wed Jun 09 11:36:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!newsfeed.nyu.edu!newsfeed.sgi.net!pitt.edu!not-for-mail From: pxpst2@vms.cis.pitt.edu (Peter) Newsgroups: bionet.molbio.proteins Subject: Re: Cell lysing for protein assay Date: Wed, 09 Jun 1999 15:29:53 -0400 Organization: University Of Pittsburgh Lines: 23 Distribution: world Message-ID: References: <9173148B8F8CD1118AAC00805F0649C66C2C61@KSCXCHG2> NNTP-Posting-Host: pelli.pathology.pitt.edu Mail-Copies-To: pxpst2@vms.cis.pitt.edu X-Newsreader: MT-NewsWatcher 2.4.4 In article <9173148B8F8CD1118AAC00805F0649C66C2C61@KSCXCHG2>, Rachael.Russell@esr.cri.nz ("Russell, Rachael") wrote: > If anyone has any ideas, please > let me know. Am currently using an EDTA/PBS/Triton X-100 buffer, but would > like to know of more possibile buffers, and methods ie how long to incubate > buffer. (I am using adherant cells in 96-well plates) 20 mM Tris pH 8 with the addition of prtease inhibitors is what I use. PBS is normal saline so yo will have to use mechanical force to break the cell open. regards, -- Peter _____________________________________________________________________ " Some of you might not agree 'Cause you probably likes a lot of misery But think a while and you will see... Broken hearts are for assholes" FZ From owner-proteins@net.bio.net Thu Jun 10 01:44:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!news.maxwell.syr.edu!nntp.news.xara.net!xara.net!server5.netnews.ja.net!news.york.ac.uk!not-for-mail From: "Peter Ashton" Newsgroups: bionet.molbio.proteins Subject: Re: how to calculate the molar absorption coefficient of a protein? Date: Thu, 10 Jun 1999 10:39:46 +0100 Organization: The University of York, UK Lines: 23 Sender: pda2@york.ac.uk Message-ID: <7jo129$9hr$1@pump1.york.ac.uk> References: <7jm7qv$ing$1@bgtnsc02.worldnet.att.net> NNTP-Posting-Host: biolpc294.york.ac.uk X-Trace: pump1.york.ac.uk 929007497 9787 144.32.84.128 (10 Jun 1999 09:38:17 GMT) X-Complaints-To: abuse@york.ac.uk NNTP-Posting-Date: 10 Jun 1999 09:38:17 GMT X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 5.00.2314.1300 X-MimeOLE: Produced By Microsoft MimeOLE V5.00.2314.1300 this should tell you what you need to know http://www.expasy.ch/tools/protparam.html Pete Bob wrote in message news:7jm7qv$ing$1@bgtnsc02.worldnet.att.net... > Is there any web site that would calculate the absorption coefficient of a > protein on the basis of the number of tryptophans, tyrosins, Phe, disulfide > bonds... > > Or if not, what is the formula? > > Thanks, Rob > > > > From owner-proteins@net.bio.net Thu Jun 10 01:54:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!dispose.news.demon.net!demon!newsfeed.nacamar.de!newsfeed.nacamar.de!news-feed.inet.tele.dk!bofh.vszbr.cz!news.inet.tele.dk!not-for-mail From: Thomas Krag Newsgroups: bionet.molbio.proteins Subject: Re: GST-fusion degradation! Date: Thu, 10 Jun 1999 12:02:19 +0200 Organization: Tele Danmark Internet Message-ID: <375F8D2B.38C1A56C@dcb-glostrup.dk> References: <01bea6f6$11907cc0$3754cc84@ribosome.bch.umontreal.ca> NNTP-Posting-Host: 194.192.80.89 Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: news.inet.tele.dk 929008123 1902 194.192.80.89 (10 Jun 1999 09:48:43 GMT) X-Complaints-To: Department of Abuse NNTP-Posting-Date: 10 Jun 1999 09:48:43 GMT X-Mailer: Mozilla 4.03 [da] (Win95; I) Lines: 49 I don't know what kind of proteins you are working with, but some of the degradation depends on the N-terminal part of the fused protein. Meaning that if you've got an N-terminal, which isn't tightly coiled up or bound to the rest of the protein with disulphide bridges, it becomes more susceptibel for proteolytic digest. It is hard to avoid this degradation, but to some instance a lowering of the temperature will do it, to 30 or 27 degrees celsius. If you lower the concentration of the inducer and instead induce twice within an hour, you may get better results as well. Nothing guaranteed though! Addition of more inhibitors like Aprotinin, pepstatin and leupeptin may help. Regarding sonication, it is probably the best method, though I know a lot of people will dispute this. But everything depends on your sonication protocol. Some of your protein may stay in the pellet after sonication, in which case you'll have to revise your protocol or you may denature the whole thing. I'm not sure the MBP-fusion system will solve the degradation issue as your problem does not seem to have anything to do with the fusionprotein, GST, itself! Regards Thomas Krag PS What cell line are you using? BL21, DH5alpha, ....? Robert, Francis skrev: > > Hi everyone, > > I'm working with GST-fusion system. For two of my fusion proteins I get > degradation of the fused part only while for others, ther is no degradation > at all. This means that the only protein I can purify is the GST alone > since it has a better affinity for the column than the fusion protein. I'm > not sure, but I think I see on a coomassie-stained gel that the degradation > occurs fisrt in the cells and continues during the course of the > purification. I use PMSF and Benzamidine. Should I use more inhibitors? > The lysis method implies sonication, should I use other lysis methods? > > Is there any magical methods that would prevent degradation like reducing > the growth temperature or the inducing time? Would the MBP-fusion system be > a better system in case of degradation. > > Thanks > > Francis R. -- From owner-proteins@net.bio.net Thu Jun 10 01:55:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!hermes.visi.com!news-out.visi.com!hub1.ispnews.com!cyc12.deja.bcandid.com!nntp1.deja.com!nnrp2.deja.com!nntp2.deja.com!nnrp1.deja.com!not-for-mail From: Kresten Newsgroups: bionet.molbio.proteins Subject: Re: how to calculate the molar absorption coefficient of a protein? Date: Thu, 10 Jun 1999 08:54:03 GMT Organization: Deja.com - Share what you know. Learn what you don't. Lines: 34 Message-ID: <7jnuf9$d2t$1@nnrp1.deja.com> References: <7jm7qv$ing$1@bgtnsc02.worldnet.att.net> <7jmcft$a4q$1@moonbeam.aecom.yu.edu> NNTP-Posting-Host: 130.226.1.36 X-Article-Creation-Date: Thu Jun 10 08:54:03 1999 GMT X-Http-User-Agent: Mozilla/4.5 [en] (Win95; I) X-Http-Proxy: 1.0 www2.crc.dk:3128 (Squid/2.1.RELEASE),NetCache@www-cache: Version 3.3.1, 1.0 x29.deja.com:80 (Squid/1.1.22) for client 130.226.182.217, 130.226.1.36 > >Is there any web site that would calculate the absorption coefficient of a NO (not yet), but there are ways of estimating them > >protein on the basis of the number of tryptophans, tyrosins, Phe, disulfide > >bonds... > > > > See the article: Gill and von Hippel, Analytical Biochemistry 182, 319-326 (1989). There has also been a more recent paper going down the same way. I cannot (sorry) find the ref. at the moment. Also see: http://www.expasy.ch/tools/protparam.html and the references at that site. HTH Kresten -- The address kresten@my-dejanews.com is for spambots only. Please mail me at LysLeuLeu@crc.dk , transforming the pre@-part into my initials. Kresten Lindorff Larsen, Dept. Yeast Genetics Carlsberg Laboratory, Denmark Sent via Deja.com http://www.deja.com/ Share what you know. Learn what you don't. From owner-proteins@net.bio.net Thu Jun 10 02:35:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!news-feed.inet.tele.dk!bofh.vszbr.cz!news.inet.tele.dk!not-for-mail From: Thomas Krag Newsgroups: bionet.molbio.proteins Subject: Re: Concentrating enzymes Date: Thu, 10 Jun 1999 12:42:54 +0200 Organization: Tele Danmark Internet Lines: 54 Message-ID: <375F96AE.CC8A3DBA@dcb-glostrup.dk> References: <3.0.1.32.19990525161510.006dbd7c@cc.usu.edu> NNTP-Posting-Host: 194.192.80.89 Mime-Version: 1.0 Content-Type: text/plain; charset=iso-8859-1 Content-Transfer-Encoding: 8bit X-Trace: news.inet.tele.dk 929010557 1902 194.192.80.89 (10 Jun 1999 10:29:17 GMT) X-Complaints-To: Department of Abuse NNTP-Posting-Date: 10 Jun 1999 10:29:17 GMT X-Mailer: Mozilla 4.03 [da] (Win95; I) Why not just dialyse the pooled batches into 20mM Tris, 0.5M NaCl , pH 7.4 or a buffer that is compatible with your enzyme, and after dialysis, let the pool recirculate on your ConA column overnight or some hours (depends on the size of your column). Elution will happen in a much smaller volume, so you may get from 200 ml pooled batch to 1½-2 ml eluted protein in two easy steps. Only problem is your requirement for concentration at an earlier step. Regards Thomas Krag Phil Harrison skrev: > > Hello all. > > I have been losing my enzyme activity when I concentrate the > enzyme and could use some help. > I am purifying a fructosyltransferase from plant tissue. After > ammonium sulfate fractionation and > desalting, I have been pooling 4-5 batches and concentrating by > an Amicon thin channel device. > These are not sold any more, so let me explain that they are > like a stirred cell, except the > enzyme solution is pumped through a thin channel tangentially > over the surface of the membrane. > Nitrogen from a compressed nitrogen tank pushes the buffer > through the membrane while the pump > recirculates the enzyme solution over the membrane. > > I am concentrating ca. 200 ml down to ca. 45 ml. Occasionally I > get ca. 90% recovery of the > enzyme activity. More often I get 20-25% recovery, and > sometimes even less. > > Can anyone suggest a method or methods for concentrating that > would be more gentle on my > enzyme? It is a glycoprotein of MW ca. 60 kD. I use a ConA > column later in the procedure, > but need concentrating steps earlier. > > Thanks in advance. > > Phil -- ******************************************************************** Thomas Krag, M.Sc Phone/work: +45 43232470 Dept. of Clinical Biochemistry Fax/work: +45 43233929 Glostrup Hospital Email/work: tk@dcb-glostrup.dk DK-2600 Glostrup Email/home: krag@post6.tele.dk Denmark ******************************************************************** From owner-proteins@net.bio.net Thu Jun 10 03:35:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!uchinews2!newsswitch.lcs.mit.edu!newsfeed.enteract.com!newsfeed.tli.de!newsfeed.nacamar.de!fu-berlin.de!news.uni-paderborn.de!news-han1.dfn.de!news.gwdg.de!not-for-mail From: Silke Beismann Newsgroups: bionet.molbio.proteins Subject: Streptomycin-preciptation Date: Thu, 10 Jun 1999 12:07:39 +0200 Organization: GWDG, Goettingen Lines: 13 Message-ID: <375F8E6B.16B5B20D@uni-molgen.gwdg.de> NNTP-Posting-Host: 134.76.70.64 Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.5 [en] (WinNT; I) X-Accept-Language: en Hi , during my protein purification I have a lot of trouble to get rid of nucleic acids. I have to use high amounts of Benzonase, dialyse extensively, use several chromatography columns and so on. Now I read in a paper a protocoll for streptomycin sulfate precipitation of nucleic acids. Has anyone used this method before? Is it mild to the protein and efficiently in respect of the nucleic acids? Thanks for your answers, Silke Beismann From owner-proteins@net.bio.net Thu Jun 10 06:41:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!remarQ73!remarQ-easT!supernews.com!remarQ.com!grolier!club-internet!not-for-mail From: thesax@club-internet.fr (Loïck Le Dantec) Newsgroups: bionet.molbio.proteins Subject: Re: GST-fusion degradation! Date: Thu, 10 Jun 1999 14:46:59 GMT Organization: Club-Internet (France) Lines: 28 Message-ID: <3766cfe2.17318286@news.club-internet.fr> References: <01bea6f6$11907cc0$3754cc84@ribosome.bch.umontreal.ca> <375F8D2B.38C1A56C@dcb-glostrup.dk> NNTP-Posting-Host: pau-6-195.club-internet.fr Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: front1m.grolier.fr 929025125 11883 195.36.133.195 (10 Jun 1999 14:32:05 GMT) NNTP-Posting-Date: 10 Jun 1999 14:32:05 GMT X-Newsreader: Forte Agent 1.01/32.397 >> >> Hi everyone, >> >> I'm working with GST-fusion system. For two of my fusion proteins I get >> degradation of the fused part only while for others, ther is no degradation >> at all. This means that the only protein I can purify is the GST alone >> since it has a better affinity for the column than the fusion protein. I'm >> not sure, but I think I see on a coomassie-stained gel that the degradation >> occurs fisrt in the cells and continues during the course of the >> purification. I use PMSF and Benzamidine. Should I use more inhibitors? >> The lysis method implies sonication, should I use other lysis methods? >> >> Is there any magical methods that would prevent degradation like reducing >> the growth temperature or the inducing time? Would the MBP-fusion system be >> a better system in case of degradation. >> >> Thanks >> >> Francis R. > >-- There's some hints inGoeddel V.(1990) Systems for heterologous gene expression. Methods in Enzymology, 185, 3-228. Periplasmic export may be used (MBP-fusion with the pMAL-p2 system) as a means to remove the protein of interest from the proteases. hth (sorry for my english) From owner-proteins@net.bio.net Thu Jun 10 09:23:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!sunqbc.risq.qc.ca!carnaval.risq.qc.ca.POSTED!not-for-mail From: "Denis LeBel" Newsgroups: bionet.molbio.proteins Subject: Promega's GeneEditor Lines: 10 X-Newsreader: Microsoft Outlook Express 4.72.2106.4 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.2106.4 Message-ID: <1rS73.7919$U4.333543@carnaval.risq.qc.ca> Date: Thu, 10 Jun 1999 17:17:49 GMT NNTP-Posting-Host: 132.210.26.30 X-Trace: carnaval.risq.qc.ca 929035069 132.210.26.30 (Thu, 10 Jun 1999 13:17:49 EDT) NNTP-Posting-Date: Thu, 10 Jun 1999 13:17:49 EDT Did anyone ever used the GeneEditor product (Promega) satisfactorily to make more than one mutation on a single plasmid? If so, I would very much like to contact this person. Thanks Denis LeBel, Biology, University of Sherbrooke From owner-proteins@net.bio.net Thu Jun 10 09:47:00 1999 Path: biosci!BILONG.COM!info From: info@BILONG.COM (BILONG Transgenics) Newsgroups: bionet.molbio.proteins Subject: '99 ISAAST. Date: 10 Jun 1999 10:47:44 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 253 Sender: daemon@net.bio.net Distribution: world Message-ID: <375FF811.3021C350@bilong.com> NNTP-Posting-Host: net.bio.net '99 International Symposium on Aging and Antiaging Science & Technology (with EXHIBITION) September 8-12, 1999 Beijing, China Scientific Sessions 1. Biological Science 2. Clinical & Experimental Medicine 3. Health Care for the Elderly 4. Traditional Chinese Medicine in Aging & Antiaging Invited Speakers: I. Biological Sciences Prof. Hajime Orimo, Japan # Osteoporosis - - - -Update *Dr. Dazhong Yin, Sweden # Free Radical, Non-enzymatic Glycosylation & Lipofuscin Prof. Zong-Yu Zhang and Tan-Jun Tong: Beijing, China # Progress in Research on Molecular Mechanisms of Aging Dr. Xu Song, Beijing, China # The Demonstration of the Thesis of Nonenzymatic Glycosylation Inducing Aging *Prof. Ayala Hochman, Tel Aviv, Isreal, £¿ # Overview of Free Radicals and Neurodegenerative diseases * Dr. Ron Kohen, Jerusalem, Israel # Reducing Equivalents in the Aging Process Prof. Beka Solomon: Tel Aviv, Isreal # Therapeutic Antibodies, a New Approach in Treatment of Alzheimer’s Disease Prof. Wen-Bin Li, Beijing, China # Aging-mimetic effect of D-galactose and its Mechanism Dr. Zhong-Ming Wen, Suzhou, China Study of Aging Model in Rats Prof. Biansheng Liu, Wuhan, China # The Relationship of Nutrition and Aging Prof. Anna Xue, Beijing, China # Study on the Induction of Apoptosis by Superoxide Anion and Inhibition Effect of Antioxidant Nutrient Dr. Andrey I. Sukhodub, Kharkiv, Ukraine # Hypothetical Mechanism of Benzene Membrane Damage Action on the Liver Microsomers£¨£¿£© from Different Age Rats Prof. Ke-ji Chen, Beijing, China # Chinese Medicine and Health Preserving Dr. Cai-min Xu, Beijing, China # The Changes of Membrane Lipids and Proteins in the Aging Process of Erythrocytes Dr. Ping Wang, Wuhan, China # Theoretical and Experimental Research on the Relationship Between Excessive Intake of Fat-sweet Food and Senility II. Geriatrics *Prof. David J.E.Callaway, New York, USA # Molecular Model of Alzheimer Amyloid Fibril Formation Prof. Rui Han, Beijing, China # Recent Progress of Anticancer Drugs Originated From Plants in China Prof. Shu-Li Sheng, Beijing, China # Advance in Pathogenic Mechanism of Alzheimer’s Disease Prof. Yong-Jie Li, Beijing, China # Progress in Surgical Treatment of Parkinson’s Disease Dr. Jinghe Li, Pharmacia & Upjohn, USA # A New Twist in Alzheimer Presenilins Prof. Geng-tao Liu, Beijing, China # Protective Action of the Extract of Gingko Biloba (EGb761) Against Oxidized Low Density Lipoprotein-induced Damage of Endothelial Cells of New Born Calf Aorta. Dr. Shi-xin Jin, Beijing, China # The Osteoporosis of Aged Male --74 Case Analysis Prof. Yong-xing Ma, Shanghai, China # Cognitive Impairment and Dementia in the Aged and Preaged : Comprehensive Mechanism and Intervention Prof. Zhu-fang Shen, Beijing, China # The Hypoglycemic Effects of a Chinese Traditional Medicine (S 2), One of the Glucosidase Inhibitors Dr. Chun-qiang Guo, Beijing, China # Effects of 9804 on Learning and Memory of Mice Dr. Ying Wang, Beijing, China # Investigation of 9804 on Some Amino Acids in Brain of Mice Dr. Jiang-guo Chen, Nanjing, China # Studies on the Relationship between the Oxidatively Modified Low Density Lipoprotein and the Aging of the Myocardial and Renal Cells in Ovariectomized Rhesus Monkey. Dr. Huaxi Xu, New York, USA # Cell Biology of Alzheimer’s Disease: Mechanism for Beta-amyloid Generation and Regulation Dr. Lan Sun, Beijing, China # Effects of Coryfolia Extract in Prevention and Treatment of Osteoporosis Dr. Feng-hua Liu, Beijing, China # The Neuprotective Effect of Estrogen and Antioxidants Against Beta-amyloid Peptides(25-35) Induced Toxicity in Cultured Neuron Cells Dr. Wei Wang, Beijing, China # Research Report on Behavior and Therapeutic Mechanism of Alzheimer’s-type Dementia Induced in Mice by Centrally Administered Beta-amyloid Peptides Yan Chen, Beijing, China # Therapeutic Effects of 764-3 on Alzheimer’s-type Dementia Induced in Rats by Centrally Administered Beta-amyloid Peptides Dr. Mengen Zhang, Beijing, China # Prevention and Therapeutic Effects of BuShenHuoXueFang on Ischemia-type Dementia in Mice Hu Zhu, Beijing, China # Combined Monitoring of CEA and TSA Value in Early Diagnosis of Lung cancer III. Traditional Chinese Medicine in Treatment of Diseases in the Elderly Dr. Jia-shi Zhu, California, USA # The Effect of Chinese Anti-aging Food/drug Corcyceps (CordyMaxTM Cs-4) Improves Steady Bio-energy Status in Mouse Liver Prof. Jun-tian Zhang, Beijing, China # Study on the Antiaging Effect of Ginsenoside Rg1 and Rb1 Prof. Junda Liu, Beijing, China # Modulate effect of Chinese Herbs on Immune Function of Lymphocytes in the Elderly Prof. Chunsheng Li, Beijing, China # Status of a Decade of Study on Anti-senility Drugs by Applying Life-experiment and Senile Animal Model in China Zhi-xin Li, Beijing, China # Comparative Study on Modulating Effects of Different Kidney-Supplementing Spleen-vigorating Stasis-Removing Decoctions on Immune Function and Free Radical Metabolism in Old Mice Prof. Zhi-qui Wu, Beijing, China #1. Molecular Study of Crystalline Modification for Preventing Senile Cataract with Chinese Herbs of Tonifying Kidney and Supplementing Blood #2. A Study of Antiaging by Chinese Medicine Herbs of Tonifying Kidney and Nurishing Blood from the View of TCM theory. Dr. Guan-hua Du and Yong-hong Chen, Beijing, China # Effects of Salvianolic acid B on the Functions of Brain Mitochondria in Aging Mice Prof. Lin Li, Beijing, China # Effects of Chinese Herbs on dementia-like animal Models and Cell Models Prof. Jin-Zhou Tian, Beijing, China #1. The Influence of Compound Fhubarb Preparation on ChAT, AChE Activities and Ach Content of Aged Mice’s Cerebral Cortex and Hippocampus. or #2. Neuropsychological Findings Preceding Alzheimer’s dementia in English Individuals with Cognitive Impairment. #3. Research into the Treatment for Vascular Dementia in China Using Traditional Chinese Therapies Dr. Jiansheng Li, Zhengzhou, China # Effect of Daihuang Zhechong Pill of TCM on Kidney TXB2 and 6-Keto-PGF12 of Patients with Early-Stage Diabetic Nephropathy in the Aged. Exhibition The companies engaged in producing the instruments or reagents that may facilitate the antiaging researches are welcomed and encouraged to exhibit their high-tech products. For whose interested in the exhibition, please contact us at your earliest convenience. Sponsor Antiaging Science & Technology Society£¬ Gerontological Society of China Organizers Antiaging Science & Technology Society , Gerontological Society of China China International Symposium Center for Sciences and Technology (CICCST) Supporters Gerontological Society of China Institute of Medicinal Biotechnology, Peking Union Medical College, Chinese Academy of medical Sciences Beijing Hospital and Gerontological Research Institute (to be continued) Contact: ********************************************************* BILONG Academic Events Add: 8 Nan Er Jie, Zhong Guan Cun, Beijing 100080, China Box: P.O. Box 8734, Beijing 100080, China Tel: 86-10-6256-0561, 6256-2226 Ext 211, 800-810-0797 Fax: 86-10-6253-2114 Email: BAE@bilong.com Website: www.ciccst.org.cn/99ISAAST ********************************************************* From owner-proteins@net.bio.net Thu Jun 10 09:47:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!cyclone.bc.net!mongol.sasknet.sk.ca!news@mongol From: "Michael R. Thompson" Newsgroups: bionet.molbio.proteins Subject: Re: Streptomycin-preciptation Date: Thu, 10 Jun 1999 11:22:12 -0600 Organization: SaskTel Lines: 29 Message-ID: <7josfm$ev05@mongol.sasknet.sk.ca> References: <375F8E6B.16B5B20D@uni-molgen.gwdg.de> NNTP-Posting-Host: pbigate.pbi.nrc.ca X-Newsreader: Microsoft Outlook Express 4.72.3110.5 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.3110.3 I have used protamine sulphate to remove nucleic acids prior to isoelectric focusing, or before purifying a recombinant enzyme. Dissolve protamine sulphate powder in buffer and neutralize (it is quite acidic) before adding to your protein prep. Use at a ratio (w:w) of about 1:30 of total protein. Shake or rotate the vessel in the coldroom for about 1 hour, spin out the precipitate afterwards. Seems to work well in both of my applications and doesn't affect the activity of the enzyme. Protamine binds to all nucleic acids, consequently it may also precipitate nucleic acid-binding proteins (handy selective purification step in some applications). It may also precipitate other proteins so you will have to check with yours. Streptomycin precipitates ribosomes quite cleanly but doesn't remove DNA. Silke Beismann wrote in message <375F8E6B.16B5B20D@uni-molgen.gwdg.de>... >Hi , > >during my protein purification I have a lot of trouble to get rid of >nucleic acids. I have to use high amounts of Benzonase, dialyse >extensively, use several chromatography columns and so on. Now I read in >a paper a protocoll for streptomycin sulfate precipitation of nucleic >acids. Has anyone used this method before? Is it mild to the protein and >efficiently in respect of the nucleic acids? > >Thanks for your answers, > >Silke Beismann > From owner-proteins@net.bio.net Thu Jun 10 12:05:00 1999 From: Cornelius Krasel Subject: Re: Streptomycin-preciptation Newsgroups: bionet.molbio.proteins References: <375F8E6B.16B5B20D@uni-molgen.gwdg.de> User-Agent: tin/pre-1.4-19990413 ("Endemoniada") (UNIX) (Linux/2.0.36 (i486)) MIME-Version: 1.0 Content-Type: text/plain; charset=ISO-8859-1 Content-Transfer-Encoding: 8bit Date: Thu, 10 Jun 1999 20:19:40 +0200 Message-ID: NNTP-Posting-Host: wpxx02.toxi.uni-wuerzburg.de Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!news-lond.gip.net!news.gsl.net!gip.net!colt.net!news0.de.colt.net!blackbush.xlink.net!uni-erlangen.de!uni-wuerzburg.de!not-for-mail Lines: 29 Silke Beismann wrote: > during my protein purification I have a lot of trouble to get rid of > nucleic acids. I have to use high amounts of Benzonase, dialyse > extensively, use several chromatography columns and so on. Now I read in > a paper a protocoll for streptomycin sulfate precipitation of nucleic > acids. Has anyone used this method before? Is it mild to the protein and > efficiently in respect of the nucleic acids? Our lab used this when purifying recombinant phosducin from E.coli before applying the supernatant to a MonoQ column. The reference is probably either Bauer PH, Müller, Puzicha M, Pippig S, Obermaier B, Helmreich EJM, Lohse MJ: Phosducin is a protein kinase A-regulated G-protein regulator. Nature 358: 73-76 (1992). or Hekman M, Bauer PH, Söhlemann P, Lohse MJ: Phosducin inhibits receptor phosphorylation by the beta-adrenergic receptor kinase in a PKA-regulated manner. FEBS Lett. 343: 120-124 (1994). However, since then the lab has switched to using his-tagged proteins, simply because the protein purification is much more convenient (no HPLC needed for same purity). Hope that helps, --Cornelius. -- /* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */ /* D-97078 Wuerzburg, Germany email: phak004@rzbox.uni-wuerzburg.de SP4 */ /* "Science is the game we play with God to find out what His rules are." */ From owner-proteins@net.bio.net Thu Jun 10 20:32:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!news.maxwell.syr.edu!news.mel.connect.com.au!news.unimelb.edu.au!ludwignt-4 From: murphy_r@licre.ludwig.edu.au (Roger Murphy) Newsgroups: bionet.molbio.proteins Subject: Re: how to calculate the molar absorption coefficient of a protein? Date: Fri, 11 Jun 99 03:29:06 GMT Organization: Ludwig Institute for Cancer Research Lines: 36 Message-ID: <7jq34u$n89$1@izvestia.its.unimelb.edu.au> References: <7jm7qv$ing$1@bgtnsc02.worldnet.att.net> NNTP-Posting-Host: ludwignt-4.austin.unimelb.edu.au X-Trace: izvestia.its.unimelb.edu.au 929075166 23817 128.250.186.193 (11 Jun 1999 04:26:06 GMT) X-Complaints-To: news@news.unimelb.edu.au NNTP-Posting-Date: 11 Jun 1999 04:26:06 GMT X-Newsreader: News Xpress 2.0 Beta #0 Sure, go to the ExPassy web site and select the proteomics tools options. There you can either load in your own sequence (paste from a text file) or a database number if the protein of interest is known, and calculate all sorts of physicochemical parameters, using a number of tools. Cheers, Roger In article <7jm7qv$ing$1@bgtnsc02.worldnet.att.net>, "Bob" wrote: >Is there any web site that would calculate the absorption coefficient of a >protein on the basis of the number of tryptophans, tyrosins, Phe, disulfide >bonds... > >Or if not, what is the formula? > >Thanks, Rob > > > > ------------------------------------------------------------ Roger Murphy, Ph.D. Biological Production Facility Ludwig Institute for Cancer Research Austin & Repatriation Medical Centre Studley Road, Heidelberg, Vic. 3084 Australia. Tel 61-3-94965463 Fax 61-3-94965436 Email Roger.Murphy@Ludwig.edu.au From owner-proteins@net.bio.net Fri Jun 11 00:49:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!dispose.news.demon.net!demon!newsfeed.nacamar.de!newsfeed.nacamar.de!fu-berlin.de!server1.netnews.ja.net!pegasus.csx.cam.ac.uk!hgmp.mrc.ac.uk!biosci From: gussak@mail.agri.gov.il (Eugene Gussakovsky) Newsgroups: bionet.molbio.proteins Subject: Re: how to calculate the molar absorption coefficient of a protein? Date: 11 Jun 1999 08:08:53 +0100 Organization: ARO Message-ID: <3760B659.50A47E8C@ias.agri.gov.il> References: <7jm7qv$ing$1@bgtnsc02.worldnet.att.net> NNTP-Posting-Host: mercury.hgmp.mrc.ac.uk Mime-Version: 1.0 Content-Type: text/plain; charset=koi8-r Content-Transfer-Encoding: 7bit X-Trace: niobium.hgmp.mrc.ac.uk 929084934 14976 193.62.192.80 (11 Jun 1999 07:08:54 GMT) X-Complaints-To: news@hgmp.mrc.ac.uk NNTP-Posting-Date: 11 Jun 1999 07:08:54 GMT X-Received: from alpha.netvision.net.il (alpha.netvision.net.il [194.90.1.13]) by hgmp.mrc.ac.uk (8.9.3/8.9.3) with ESMTP id IAA02120 for ; Fri, 11 Jun 1999 08:08:49 +0100 (BST) X-Received: from mail.agri.gov.il (mariana.agri.gov.il [62.0.34.66]) by alpha.netvision.net.il (8.9.3/8.8.6) with ESMTP id KAA18594; Fri, 11 Jun 1999 10:08:47 +0300 (IDT) X-Received: from ias.agri.gov.il by mail.agri.gov.il (8.8.8/1.1.22.3/20May99-1040AM) id KAA0000021205; Fri, 11 Jun 1999 10:06:07 +0300 (IDT) X-Reply-To: gussak@mail.agri.gov.il X-Mailer: Mozilla 4.5 [en] (Win95; I) X-Accept-Language: en X-To: Bob X-CC: proteins@hgmp.mrc.ac.uk Lines: 27 Bob wrote: > Is there any web site that would calculate the absorption coefficient of a > protein on the basis of the number of tryptophans, tyrosins, Phe, disulfide > bonds... > > Or if not, what is the formula? > > Thanks, Rob Hi, Rob, Try a good paper by Pace et al. (1995) in Protein Science 4,2411-2423. But pay attention that there are no any method to exactly calculate an extinction coefficient. A calculated value can be used for estimation only (however the estimation may be quite good!). I'd recommend to measure (i) using Biuret or other absolute method of the protein concentration determination and (ii) applying a procedure for light scattering subtraction at the absorption spectra determination. Best wishes Eugene --- From owner-proteins@net.bio.net Fri Jun 11 18:28:00 1999 Path: biosci!GOLDRUSH.COM!geos From: geos@GOLDRUSH.COM ("george sibbald") Newsgroups: bionet.molbio.proteins Subject: Scientfic review article AFM in Biology 1999 Date: 11 Jun 1999 19:28:47 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 16 Sender: daemon@net.bio.net Distribution: world Message-ID: <032f01beb47a$28300cc0$74c0dad1@sibbald> Reply-To: "george sibbald" NNTP-Posting-Host: net.bio.net Review article on SPM in Biology! First draft, posted for comments/feedback only, final version will be published by John Wiley in the book "Scanning Tunneling Microscopy and related techniques" ed. D. Bonnell. Author: Prof. Stuart Lindsay, ASU View the Article here. http://green.la.asu.edu/index.html From owner-proteins@net.bio.net Sat Jun 12 20:30:00 1999 Newsgroups: alt.support.cancer,bionet.molbio.gene-linkage,bionet.molbio.proteins Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!news.new-york.net!uunet!ffx.uu.net!world!sphinx From: sphinx@world.std.com (SPHINX Technologies) Subject: Re: Your cancer cure! Message-ID: Date: Sun, 13 Jun 1999 04:22:47 GMT References: <37616cf1.109178972@news.mindspring.com> <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net> Organization: SPHINX Technologies, Inc., Wellesley Hills, MA Lines: 227 Xref: biosci bionet.molbio.gene-linkage:2083 bionet.molbio.proteins:14457 In article <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net>, Nancy Luft wrote: >normal healthy cells [and] tumor cells are undifferentiated cells. >Embryonic cells in an embyro are also undifferentiated cells. Normal >healthy cells are adult cells or differentiated cells. > >What is the difference between the two types? Undifferentiated cells in >neoplasms and embryos both lack the organelles of mature, healthy cells. >Organelles are tiny structures of cells that allow a cell to carry on >the functions of adult, mature, differentiated cells. Undifferentiated >cells are immature cells that can not carry on the functions of mature >cells. Presumably you mean that undifferentiated cells lack SOME of the organelles of adult differentiated cells. I would think that all cells would have ribosomes, which are the organelles responsible for manufacturing proteins. Or, as I have learned recently, more precisely, for translating the codes for proteins in DNA (after its transcription into RNA) into the corresponding protein. The basic protein molecule is then, more often than not, "edited" into a slightly different final form by subsequent chemical reactions. (This can include splitting a protein into two or more sub-chains, so "slightly" isn't always strictly accurate.) >Cone Cancer Treatment, from what I gather not knowing much abut it, is >very similar to what the Gerson Institute uses, in some basic ways. This certainly seems to be correct, from my reading of descriptions of the two methods. >They both increase metabolism with the use of thyroid hormone, but I do >not think it is the increaed metablism per se that actually cures their >patients. Several people who have tried to apply Warburg's theory seem to think that it is the competition for glucose that deprives the cancer cells of their source of fuel. However, they may not be understanding all aspects of the process. >The Pac Man Action of immune cells is their ability to eat up and >destroy the bad guys, microbes, cancers, etc., it is called their >phagocytic action that takes place inside of phagocytic immune cells. >It is caused by a chemical reaction inside of tiny organelles or tiny >sacs inside of those phagocytic immune cells called phagosomes. That >chemical reaction in those tiny phagosomes is called the Klebanoff >Syndrome or The hydrogen peroxide + myeloperoxidase + halide system. >The halide is an iodine anion in the equation. So the late Dr. Max >Gerson fed his patients iodine to help their immune systems to work. > >In that above chemical equation is myeloperoxidase, which is an enzyme. >Enzymes are made of proteins. From what I have read, most enzymes ARE proteins. >Thyroid hormone is necessary in order for >the human body to make hundreds of different kinds of proteins that act >as enzymes, act as ion pumps (channels), and act as carrier proteins. I would be interested to learn where thyroid hormone is needed in this process. After reading this statement or one like it in an earlier post, I did some more reading and learned more about the protein synthesis process. In particular, I learned, as I noted above, that synthesis by the ribosomes is not always, maybe even not usually, the end of the process. So post-processing to edit the basic ribosome-produced protein into the final form is one place I can imagine that thyroid hormone could be needed. The other is kind of interesting. It turns out that ribosomes are themselves complexes -- it's not entirely clear from Stryer's "Biochemistry" if they are actually molecules or strings of molecules bonded together in some way -- anyway they are made up of sections which are basically RNA and are called ribosomal RNA, and sections which are proteins. Already in 1994 when Stryer's 4th Edition was published, the structure of ribosomes was known in great detail and doubtless even more is known today. Anyway, what I found fascinating was to realize that (1) Ribosomes are the "factories" that make proteins (or at least make the preliminary forms), and (2) Ribosomes themselves are partly made up of proteins. Which leaves us with a sort of "chicken and egg" problem, doesn't it? I.e., how can ribosomes get made in the first place if ribosomes are needed to make protein, but ribosomes CONTAIN protein? That is why a bare planet with just some DNA could not have life spring up very easily. As a minimum, I would think it would require a single cell containing both the DNA and a ribosome, plus some amino acids floating around. But that's digressing too much. Back to my question -- can you fill me in on how the thyroid hormone is used in the process of making myeloperoxidase? >Best I have been able to research is that the human body can not make >that needed myeloperoxidase enzyme unless it has enough thyroid hormone >to do so. So Gerson, and I was told also Cone, use thyroid hormone so >their patients can make the needed myeloperoxidase enzyme that their >patients must have in order for their phagocytic immune cells to attack >cancers. > >From my research thus far, Gerson, and perhaps Cone, have the highest >cure rates for incurable cancers, because of their use of thyroid >hormone, etc.. This is VERY interesting especially in the light of your "do-it-yourself" formula for getting the thyroid producing more thyroxin, because your method does NOT require the assistance of an M.D. (although supervision would probably be wise). >Folks with advanced cancers do not have a normal imflammation reaction >like healthy folks because they immune systems refuse to work and often >die as a result of infections because their immune systems refuse to >work. They have too much sodium and not enough potassium inside of >every cell in their bodies, also, undoubtably caused by a lack of >sodium-potassium ion pumps (channels) ... which is caused by a lack of >thyroid hormone. Their nervous systems do not work properly either >caused by a lack of neurotransmitters, ie., dopa, dopamine, adrenalin, >and noradrenalin, which are made from from an amino acid called >tyrosine. An enzyme in the liver converts the amino acids phenylalanine >into the amino acids tyrosine which is then converted into those missing >neurotransmitters. Folks with cancers lack that enzyme to convert >phenylalanine into tyrosine because they lack thyroid hormone that is >necessary to make that enzyme. Interesting... I wonder if your method of souping up thyroid function would also help people with phenylketonuria or those with difficulty processing NutraSweet(tm)? Which metabolizes into phenylanaline among other things. >When a person eats proteins the proteins get broken down into amino >acids in the digestive system and then they enter the blood system and >are taken the liver when they are deaminated, ie., in the presense of an >enzyme the ammonia group is removed from the amino acids ... which later >ends up in the urine and gives urine its smell of ammonia. Folks with >advanced cancers can not tolerate proteins much at all because that lack >that enzyme needed to deaminate amino acids ... because they lack >thyroid hormone which is necessary to produce that enzyme. What you describe here must apply to amino acids which are not needed or which are present in excess, because the body needs an "amino acid pool" to be used to synthesize proteins. >In order for the body to produce thyroid hormone it needs a bit of >Vitamin E, some iodine, and the amino acid tyrosine. Folks with >advanced cancers lack the enzyme in their livers to convert the amino >acid phenylalanine into the amino acid tyrosine, so they can not produce >enough thyroid hormone. Right they lack that given enzyme that is >needed to convert phenylalanine into tyrosine because they need thyroid >hormone to make that enzyme! So many folks with cancers just spiral >down hill until DEATH. > >Well, after reading, researching, going through endess hell and >confusion, I learned the above information. And I took 1000 mgs. of >L-tyrosine I purchased at a GNC store, plus a bit of Vitamin E, never >more the 100 IU's per day, and seven times the daily recommended dose of >iodine, never take more then ten times the daily recommended dose of >iodine or it shuts down your thyroid, and I got my immune system to >function and wipe out cancers, and infections for me! Interestingly, Adelle Davis in "Let's Get Well" claims that adequate vitamin E intake can also facilitate REPAIR of damaged (scar) tissue in the thyroid, the liver, the kidneys, and elsewhere. I think she would suggest a higher dose that 100 IUs. Also, research reported a few years ago by the Tufts University Center on Nutrition and Ageing said that their data showed 800 IU/day to be "cancer-protective". They also said that preliminary results suggested that only 400 IU/day would also have a cancer-protective effect but that they did not feel confident in stating that result positively at that time. All dosages should be scaled to the patient's body volume, hence more or less to mass or weight, because the substance be it drug or vitamin gets diluted throughout the volume of the body. But anyway, for average-sized people, I would think that 400 IU would be a good dosage of vitamin E. Did you have a reason for limiting it to 100 IU? > Yup, I got my >thyroid to make its own hormone. I now retain potassium, I can eat >proteins again, etc., also. If doing what I did, always take your pulse >and temperatue and record it. If your pulse gets too rapid or your >temperature too high, stop temporary or reduce the downward the doses. >I thought my approach much safer then using unsupervised thyroid >hormone. When giving a patient thyroid hormone supplements, a smart doctor will usually not wait for the symptoms you mention, but will "read the body's theromostat", i.e. prescribe a test for TSH, or Thyroid-Stimulating Hormone, level in the blood. This is the body's signal that asks for more thyroxin to be made. It would probably be the best way to determine how your method was working, too, and to guide you in chages of dosage of tyrosine/iodine/vit E. >If you read a lot of health books you learn that both chloride and >The best thus far I have come up with for folks that have active >cancers is to combine an anti egg diet with what I did or a combination >of iodine and thyroid hormone ... the latter I do not like folks using >without medical supervision, ie., using tyrosine, a bit of E, and some >small amount of iodine is much safer as I did. It would be interesting to see what would be the effect of oxygen in context with thyroid extract. My hunch, for what it's worth, is that having an adequate oxygen level present would be helpful too, although the thyroxin level might well also be necessary to stimulate the aerobic cells to USE the oxygen. >Gerson's book, A Cancer Therapy, used potassium supplements because of >the lack of potassium in every cell in the body in his cancer patients. >If you do that, just remember that potassium suppements will block the >absorption of B-12 and cause anemia, therefore you must take B-12 >supplements with the potassium supplements. Or eat lots of steam cooked >potatoes, winter squash, bananas, orange or grapefruit juice, ... foods >rich in potassium. > >Well, I must end this, but I hope you understand the pure science when I >CAUTION cancer folks about eating things that reduce the amount of >iodine in their bodies, now. I for one appreciate your comments. You've alerted me to the fact that limiting CHLORIDE (and fluoride) intake may be more important than limiting SODIUM intake! And I applaud your efforts to understand, as you said, why these dietary cancer therapy methods work when they do work, and why they don't when they don't. If we could only get the mainstream oncology research community to look at this question instead of calling all non-mainstream cures "spontaneous" remissions, we would begin to see more progress toward a repeatable cure for cancer. -John Sangster Wellesley Hills, MA From owner-proteins@net.bio.net Sun Jun 13 01:00:00 1999 Path: biosci!internet!biosci!not-for-mail From: biohelp (BIOSCI Administrator) Newsgroups: bionet.molbio.proteins Subject: BIOSCI/bionet miniFAQ & Fundraiser Date: 13 Jun 1999 02:00:18 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 233 Sender: daemon@net.bio.net Distribution: world Message-ID: <199906130900.CAA21704@net.bio.net> NNTP-Posting-Host: net.bio.net (LAST REVISION: 30-JUL-95) This BIOSCI "miniFAQ" is designed to answer the questions that come up the *most frequently*. The main BIOSCI FAQ (Frequently Asked Questions) is accessible on the World Wide Web at URL http://www.bio.net/. If you can not find an answer to your question in this or other documentation, the BIOSCI technical support staff answers e-mail queries sent to biosci-help@net.bio.net We can only answer questions about the use of the newsgroups and mailing lists. We unfortunately do not have the staff to do Internet information searches or answer scientific questions. Please post those to the appropriate BIOSCI/bionet newsgroups. Contents: -------- 0) BIOSCI NEEDS YOUR SUPPORT!! 1) Using the WWW to access the BIOSCI/bionet newsgroups. 2) What to do about "spams," i.e., junk mail, ads, etc. 3) Examples of subscribing and unsubscribing to the mailing lists. 4) The BIOSCI user address and research interest directory. 0) BIOSCI NEEDS YOUR SUPPORT!! ------------------------------ BIOSCI's government funding has been expended, and we are now operating solely from advertising revenue that we have raised from our Web site at http://www.bio.net/. We need just a few minutes of your time to help us serve you. You can do two important things which will take very little time for you individually and will immensely help us continue to help you. First, please use our WWW system at http://www.bio.net/ to access the archives. You can post or reply to messages via your Web browser as described in item #1 below. Your usage helps attract sponsors. If you contact any of our sponsors, please be sure to thank them for supporting BIOSCI. It is critical for them to get this feedback if they are to continue their sponsorship for the long term. Second, if you work for a company or organization that provides products or services of interest to the biology community, please pass this message on to your marketing or marketing communications department or other appropriate group. Please ask them to help support BIOSCI by sponsoring our Web site and explain the uses and benefits of the system to the biology community. If they are interested, they can then contact us for further information at our tech support address, biosci-help@net.bio.net. 1) Using the WWW to access the BIOSCI/bionet newsgroups. -------------------------------------------------------- As of 10 December 1995, all BIOSCI/bionet full newsgroups are accessible through the World Wide Web (WWW) at URL http://www.bio.net. One can read and reply publicly or privately to both recent postings and archived messages through one's Web browser if it is configured properly to send e-mail. Each newsgroup is equipped with its own WAIS index. The main BIOSCI home page also has access to the BIO-JOURNALS Table of Contents database WAIS index and the BIOSCI user address database described in another item further below. 2) What to do about "spams," i.e., junk mail, ads, etc. ------------------------------------------------------- BIOSCI is a set of parallel USENET newsgroups (the "bionet" groups), mailing lists, and a hypermail archive at URL http://www.bio.net/. The same postings are distributed on all media (except for a small number of mailing-list-only groups at net.bio.net). Unfortunately it is becoming a despicable practice on the Internet (by a few people out to make a fast buck) to do automated mass postings to thousands of newsgroups and mailing lists. These attempts to grab free advertising are refered to as "spams" in the usual, somewhat boneheaded, net terminology. USENET is more susceptible to this practice, and many spams originate on the USENET groups and then are passed on to the mailing lists. However, spammers also get lists of mailing addresses and hit these too, so neither medium is immune. What should you do personally if you get junk mail? --------------------------------------------------- Just delete it and move on without reading it further. Filing a protest is becoming increasingly useless because spammers are often disguising the addresses where the messages are sent from. Unless you really understand Internet mail systems, your attempt at protest by sending replies to the message will often end up being sent to the address of an innocent person that the spammer is victimizing. What can BIOSCI/bionet do to protect its newsgroups? ---------------------------------------------------- The only solution currently available is to moderate the newsgroup. If this newsgroup is already moderated, then you are in good shape. Moderation protects the USENET distribution from about 95% of the spams that are being sent to date and protects the mailing lists completely. Moderation means, however, that someone has to take the time to review each message before it goes out. We have set up software here that simply allows the moderator to forward to an address at net.bio.net messages that (s)he wishes to have distributed. This takes no more time than that needed to read the message and pass it on, say about 1 min. per message. Most newsgroups currently have a discussion leader who is responsible for their newsgroup. The discussions leaders and their e-mail addresses are listed in the BIOSCI Information Sheet which is available on the Web at http://www.bio.net/. If a newsgroup is being hit with too many junk postings, please contact the discussion leader for that group and see if there is interest in moderating the group. Please do not assume that by simply posting a complaint to the newsgroup itself, anyone on the BIOSCI staff will act on your complaint. With close to 100 newsgroups to run, the BIOSCI staff has to rely on the discussion leaders of each newsgroup to report problems directly to us at biosci-help@net.bio.net. We will moderate any of our newsgroups if the discussion leader tells us that the readership of the group wishes to do so and if a moderator is willing to do the work. For most BIOSCI/bionet groups, this entails only a few minutes of work each day. Moderating a newsgroup will resolve probably 95% of the junk postings on the USENET distribution. Unfortunately there are easy ways for determined spammers to override the moderation mechanism on USENET, but we can protect our e-mail subscribers from unwanted postings if the newsgroup is moderated. You can also access our newsgroups over the WWW at URL http://www.bio.net. While this Web interface will not stop spammers from trying to post to the groups, this will give you yet another way, besides using USENET news, to keep the junk out of your personal mail files. For those of you with local USENET news systems, the Web interface will also give you faster access to new newsgroups and recent postings. 3) Examples of subscribing and unsubscribing to the mailing lists. ------------------------------------------------------------------ PLEASE NOTE: The BIOSCI management does NOT act on subscription/unsubscription requests that are posted improperly to the newsgroups and mailing lists. People who do this only bother everyone on the lists to no avail. Please be sure to follow the proper procedures below. Gory details are in the BIOSCI Information sheets on the Web at http://www.bio.net. Below we give an example utilizing the METHODS-AND-REAGENTS list at both of our two BIOSCI sites: Users in the Americas and Pacific Rim countries who use the BIOSCI ------------------------------------------------------------------ node at computer net.bio.net: ---------------------------- A) Determine the "listname" which is the <=8 character mail address ^^^^^^^^^^^^^ for the group. These can be found in the BIOSCI Info. Sheet. For the METHODS-AND-REAGENTS group the mailing address is methods@net.bio.net. The listname is the portion of the address to the left of the @ sign, i.e., "methods". The listname is used with the "subscribe" and "unsubscribe" commands illustrated below. B) Mail all commands in the body of a mail message addressed to biosci-server@net.bio.net. Do NOT send commands to the newsgroup posting addresses! 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Because of our limited personnel resources, we ask that you resubmit a *complete* form to revise your entry; we only replace complete entries and do not have resources to edit old forms. From owner-proteins@net.bio.net Sun Jun 13 22:20:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!arclight.uoregon.edu!hammer.uoregon.edu!newsfeed.direct.ca!newsfeed.concentric.net!newsfeed.clear.net.nz!ihug.co.nz!not-for-mail From: "Ross Prestidge" Newsgroups: bionet.molbio.proteins Subject: kuyfyfifkif Date: Thu, 10 Jun 1999 21:54:14 +1200 Organization: The Internet Group Ltd Lines: 3 Message-ID: <7k26l7$222$1@newsource.ihug.co.nz> NNTP-Posting-Host: p18-max7.akl.ihug.co.nz X-Newsreader: Microsoft Outlook Express 4.72.2106.4 X-MimeOLE: Produced By Microsoft MimeOLE V4.72.2106.4 fxcugtdc,f,yvf,fcdcdgt From owner-proteins@net.bio.net Mon Jun 14 07:18:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!logbridge.uoregon.edu!sunqbc.risq.qc.ca!newsflash.concordia.ca!pitt.edu!not-for-mail From: pxpst2@vms.cis.pitt.edu (Peter) Newsgroups: alt.support.cancer,bionet.molbio.gene-linkage,bionet.molbio.proteins Subject: Re: Your cancer cure! Date: Mon, 14 Jun 1999 11:11:39 -0400 Organization: University Of Pittsburgh Lines: 349 Message-ID: References: <37616cf1.109178972@news.mindspring.com> <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net> NNTP-Posting-Host: pelli.pathology.pitt.edu Mail-Copies-To: pxpst2@vms.cis.pitt.edu X-Newsreader: MT-NewsWatcher 2.4.4 Xref: biosci bionet.molbio.gene-linkage:2086 bionet.molbio.proteins:14461 In article , sphinx@world.std.com (SPHINX Technologies) wrote: > In article <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net>, > Nancy Luft wrote: > >normal healthy cells [and] tumor cells are undifferentiated cells. > >Embryonic cells in an embyro are also undifferentiated cells. Normal > >healthy cells are adult cells or differentiated cells. Normal cells may or may not be differentiated. Those words have little to do with each other. For example, the bone marrow houses fully differeintiated cells (ie osteoclasts, octeoblasts osteocytes and others) it also houses blood precussor cells which are at various levels of differentiation. Embryonic cells are generally considered to be undifferentiated when the embryo is still in the "early blast stages" but once the somites appear they are now beginning to differentiate into endoderm, ectoderm and mesoderm. And depending on the location of the cells, induction to diferentiate starts to happen by intaeraction of Mesoderm with endo/ectoderm or any combination of layers. This is a crude explination,BTW. > > > >What is the difference between the two types? Undifferentiated cells in > >neoplasms and embryos both lack the organelles of mature, healthy cells. > >Organelles are tiny structures of cells that allow a cell to carry on > >the functions of adult, mature, differentiated cells. Undifferentiated > >cells are immature cells that can not carry on the functions of mature > >cells. All organelles exsit within all cell types but there ratio to total cell volume may change over time depending on the differentiaion state of the cell. For example, a resting B-cell will apppear small and condensed. It still has all the organelles but since they are not needed they "appear without under a light microscope but can be seen with the electron microscope. Once the B-cell is stimulated, it enlarges greatly and everything can be seen under a light microscope. Once again this is a gross oversimplification. > > Presumably you mean that undifferentiated cells lack SOME of the organelles > of adult differentiated cells. I would think that all cells would have > ribosomes, which are the organelles responsible for manufacturing proteins. > Or, as I have learned recently, more precisely, for translating the codes > for proteins in DNA (after its transcription into RNA) into the corresponding > protein. The basic protein molecule is then, more often than not, "edited" > into a slightly different final form by subsequent chemical reactions. > (This can include splitting a protein into two or more sub-chains, so > "slightly" isn't always strictly accurate.) Here you are correct. All the organelles are there but enzymes required to do some of the post translational modifications may not be present in the imature cell. For example, a hepatoblast(hepatocyte precurssor and I am using this term lightly) does not express the enzyme responsible for gamma carboxylation of coagulation enzymes. Therfore even though some coagulation factor X is expressed at very low levels it is not gamma carboxylated. What is actually going on at this level is modulation of transcription factors. Whether or not a protein is expressed is dependant on the existance of the proper transcription factors which will drive its promoter. Currently, scientist are striving to understand more about transcription factors but we have a long long long way to go. > > >Cone Cancer Treatment, from what I gather not knowing much abut it, is > >very similar to what the Gerson Institute uses, in some basic ways. > > This certainly seems to be correct, from my reading of descriptions of > the two methods. > > >They both increase metabolism with the use of thyroid hormone, but I do > >not think it is the increaed metablism per se that actually cures their > >patients. This is one way to treat cancer but will not work on all tpes of cancer rather just a small subset of cancers. TH is T3 which is a ligand to a transciption factorcalled the thyroid hormone recepror. Once T3 binds to its receptor the complex then binds to a promoter element and cranks up the production of various genes that have the proper regulatory sequence in its promoter. Since T3 is distributed by the blood it will act systemically. If this is inappropriate for the cell due to altered metabolism or something else, then the cell will realize that something is wrong and will trigger a suicide program and lead to cell death by apoptosis. I think it is important at this point to define what makes a cell cancerous. A cancer cell is a cell who has mutated genomic DNA. In order for the cancer to destroy the organism, it must learn many new tricks. It must learn how to live move, it must learn how to eat through basement membranes, it must learn how to induce vasculatature, it must learn how to move into the vasculature, it must learn how to survive in the blood, it must learn how to get out of the vasculature and finally it must learn how to live and grow in another site. All in all many genes need to be hit genetically as to allow their in appropriate expression. I hope you are realizing that cancer is a difficult thing to completly understand and it is a very complex process. I do not believe that any one " magic bullet" exists to cure all cancers. Most advanced cancers have very screwed up DNA. If you looked at the chromasomes, you would see many breaks and repairs and chromasome pieces may be located in inapropriate locations. This is all very cursory explination, if you want more info, I would be happy to direct to it. > > Several people who have tried to apply Warburg's theory seem to think that > it is the competition for glucose that deprives the cancer cells of their > source of fuel. However, they may not be understanding all aspects of > the process. This is putting it mildly. > > >The Pac Man Action of immune cells is their ability to eat up and > >destroy the bad guys, microbes, cancers, etc., it is called their > >phagocytic action that takes place inside of phagocytic immune cells. > >It is caused by a chemical reaction inside of tiny organelles or tiny > >sacs inside of those phagocytic immune cells called phagosomes. That > >chemical reaction in those tiny phagosomes is called the Klebanoff > >Syndrome or The hydrogen peroxide + myeloperoxidase + halide system. > >The halide is an iodine anion in the equation. So the late Dr. Max > >Gerson fed his patients iodine to help their immune systems to work. Immune cells are quite specific on what is a target. Immune cells do not just go out and kill. And the phagocytic machinery/cells are different then the cells that kill. The cells that kill are either cytotoxic T cells or NK cells. In the case of T cell, there is a specific receptor that identifies abnormal proteins and upon recognition, it starts to perforate the cell and kill it. Then the Phagocytic cells come along and clean up the debris. For NK cells it is not known how the target is identified but it is specific and does pierce the membrane. Current strategies that want to use the immune system invlove the removing of T cells from the patient and stimulating them in the precense of cancer cells till one can be found that recognizes the cancer cell. This cell is then grown and reingected into to patient. Variants of this involve the the use of cytokines that stimulate the t cells in the persons body. See work by Michael Lotz at University of Pittsburgh. > > > >In that above chemical equation is myeloperoxidase, which is an enzyme. > >Enzymes are made of proteins. > > From what I have read, most enzymes ARE proteins. All enzymes are proteins except for ribozymes. But some interesting enzymes exsist that are a compbination of Nucleic acid and protein(see telomerase) and sine it is the belief of the scientific community that telomerase is important to stabilizing the ends of DNA, it is VERY important to cancer. > > >Thyroid hormone is necessary in order for > >the human body to make hundreds of different kinds of proteins that act > >as enzymes, act as ion pumps (channels), and act as carrier proteins. > > I would be interested to learn where thyroid hormone is needed in this > process. After reading this statement or one like it in an earlier post, > I did some more reading and learned more about the protein synthesis > process. In particular, I learned, as I noted above, that synthesis by > the ribosomes is not always, maybe even not usually, the end of the process. > So post-processing to edit the basic ribosome-produced protein into the > final form is one place I can imagine that thyroid hormone could be needed. Learn what T3 is and then think about he problem. I stated above the basics. What you need to do is see what cells are responsive to it. > > The other is kind of interesting. It turns out that ribosomes are themselves > complexes -- it's not entirely clear from Stryer's "Biochemistry" if they > are actually molecules or strings of molecules bonded together in some way -- > anyway they are made up of sections which are basically RNA and are called > ribosomal RNA, and sections which are proteins. Already in 1994 when > Stryer's 4th Edition was published, the structure of ribosomes was known > in great detail and doubtless even more is known today. Anyway, what I > found fascinating was to realize that > Ribozomes are made of many proteins not just one that come to gether as subunits. For more info get a cell biology book. I would suggest Darnell, Lodish and Baltimores "Molecular Cell Biology" > (1) Ribosomes are the "factories" that make proteins (or at least make > the preliminary forms), and Ribosomes are platforms where mRNA is read and corresponding tRNA can dock. > > (2) Ribosomes themselves are partly made up of proteins. Ribosomes are all protein but the RNA that dock there are not. :-) > > Which leaves us with a sort of "chicken and egg" problem, doesn't it? > I.e., how can ribosomes get made in the first place if ribosomes are > needed to make protein, but ribosomes CONTAIN protein? That is why > a bare planet with just some DNA could not have life spring up very easily. > As a minimum, I would think it would require a single cell containing > both the DNA and a ribosome, plus some amino acids floating around. You are now moving into evollution and how it all came to be. The current theory is that RNA came first then DNA and then protein but this is just theory and conjecture. Remember what I mentioned above the RNA can act as an enzyme and it is called a ribozyme. > > But that's digressing too much. Back to my question -- can you fill me in > on how the thyroid hormone is used in the process of making myeloperoxidase? > > >Best I have been able to research is that the human body can not make > >that needed myeloperoxidase enzyme unless it has enough thyroid hormone > >to do so. So Gerson, and I was told also Cone, use thyroid hormone so > >their patients can make the needed myeloperoxidase enzyme that their > >patients must have in order for their phagocytic immune cells to attack > >cancers. see article: Piedrafita FJ. Molander RB. Vansant G. Orlova EA. Pfahl M. Reynolds WF. An Alu element in the myeloperoxidase promoter contains a composite SP1-thyroid hormone-retinoic acid response element. Journal of Biological Chemistry. 271(24):14412-20, 1996 Jun 14. > > > >From my research thus far, Gerson, and perhaps Cone, have the highest > >cure rates for incurable cancers, because of their use of thyroid > >hormone, etc.. This is highly speculative on your part. I see no evidence this far to say that the non specific poly nuclear leucocytes are the ones killing the "cancer cells". It is entirely possible that the T3 is acting on the cancer cell and inducing oxidative stress on those cells and thus causing the cells to die via apoptosis. > > This is VERY interesting especially in the light of your "do-it-yourself" > formula for getting the thyroid producing more thyroxin, because your > method does NOT require the assistance of an M.D. (although supervision > would probably be wise). > > >Folks with advanced cancers do not have a normal imflammation reaction > >like healthy folks because they immune systems refuse to work and often > >die as a result of infections because their immune systems refuse to > >work. They have too much sodium and not enough potassium inside of > >every cell in their bodies, also, undoubtably caused by a lack of > >sodium-potassium ion pumps (channels) ... which is caused by a lack of > >thyroid hormone. Is it? please explain your logic. you can not just say that it A caused B and B caused C threfore the reason for elevation of C is due to Z without proof. T3receptor is a permiscous nuclear receptor that can pair with RXR, RAR and others and bind to sp1 sites. Which partner it binds to will define the effect. Therefore, how do you know it is not the partner to T# receptor that is the culprit? > >Their nervous systems do not work properly either > >caused by a lack of neurotransmitters, ie., dopa, dopamine, adrenalin, > >and noradrenalin, which are made from from an amino acid called > >tyrosine. An enzyme in the liver converts the amino acids phenylalanine > >into the amino acids tyrosine which is then converted into those missing > >neurotransmitters. Folks with cancers lack that enzyme to convert > >phenylalanine into tyrosine because they lack thyroid hormone that is > >necessary to make that enzyme. This is right and WRONG. Metabolism is not so clear cut. The body prefers to get its amino acids from food and adsorbs them uniformly. What you are describing is a scavenger system which may or may not be used. Also, if the enzyme is missing, it presumably is not being made and one must first speculate that the the promoter of the enzyme is not being properly stimulated which takes us back to transcription factors and which ones are or are not there. > > Interesting... I wonder if your method of souping up thyroid function > would also help people with phenylketonuria or those with difficulty > processing NutraSweet(tm)? Which metabolizes into phenylanaline among > other things. > > >When a person eats proteins the proteins get broken down into amino > >acids in the digestive system and then they enter the blood system and > >are taken the liver when they are deaminated, ie., in the presense of an > >enzyme the ammonia group is removed from the amino acids ... which later > >ends up in the urine and gives urine its smell of ammonia. Folks with > >advanced cancers can not tolerate proteins much at all because that lack > >that enzyme needed to deaminate amino acids ... because they lack > >thyroid hormone which is necessary to produce that enzyme. Folks with advanced cancers.....were these cancers treated or untreated? Many chemothearapuetic agents severly impair liver function. Thius if someone has been treated then one would expect decreasedliver function. > > What you describe here must apply to amino acids which are not needed or > which are present in excess, because the body needs an "amino acid pool" > to be used to synthesize proteins. Most correct. > > >In order for the body to produce thyroid hormone it needs a bit of > >Vitamin E, some iodine, and the amino acid tyrosine. Folks with What they need is TSH (tyroid stimulating hormone) from the pituitary. > >advanced cancers lack the enzyme in their livers to convert the amino > >acid phenylalanine into the amino acid tyrosine, so they can not produce > >enough thyroid hormone. Right they lack that given enzyme that is If that is so then one should be able to measure the tyrosine in the blood and note a " marked" decrease. I have not seen such data. Do you have it? > >needed to convert phenylalanine into tyrosine because they need thyroid > >hormone to make that enzyme! So many folks with cancers just spiral > >down hill until DEATH. The rate limiting ingredient for TH production is iodine and TSH. > > > >Well, after reading, researching, going through endess hell and > >confusion, I learned the above information. And I took 1000 mgs. of > >L-tyrosine I purchased at a GNC store, plus a bit of Vitamin E, never > >more the 100 IU's per day, and seven times the daily recommended dose of > >iodine, never take more then ten times the daily recommended dose of > >iodine or it shuts down your thyroid, and I got my immune system to > >function and wipe out cancers, and infections for me! Wooooooo. Your are now treading into the danger zone. First, I doubt that the liver allows for the tyrosine to escape to the serum. and if it did, you may run into toxicity problems. see : Yokogoshi H. Effect of dietary level of protein or methionine and threonine on the amino acids and catecholamines in brain of rats fed a high tyrosine diet. Journal of Nutritional Science & Vitaminology. 31(5):519-31, 1985 Oct. or Datta K. Ghosh JJ. Effect of dietary threonine supplementation on tyrosine toxicity in the rat. Journal of Nutrition. 107(9):1575-82, 1977 Sep Many more references can be found. If I were you, I WOULD STOP EXPERIMENTING ON YOURSELF. You are putting yourself at risk and do not have the knowledge base needed to create your own anti cancer therapy. If you want my opinion, eat lots of beans, I have seen studies that show that peaple with high intake of beans have low matastasis rates. Remeber that primary cancers do not kill it is the ones that get out that do. The rest was snipped because I could not take any more. Please do not experiment on onesself without a doctor because it is a bad idead is all I can say Regards Peter Pediaditakis Dept of Pathology University of Pittsburgh From owner-proteins@net.bio.net Mon Jun 14 08:06:00 1999 Path: biosci!WSUNIX.WSU.EDU!arthurr From: arthurr@WSUNIX.WSU.EDU (arthur roberts) Newsgroups: bionet.molbio.proteins Subject: Site with many links to protein search and analysis Date: 14 Jun 1999 09:06:45 -0700 Organization: Institute of Biological Chemistry Lines: 47 Sender: daemon@net.bio.net Distribution: world Message-ID: <3765268B.BB524B42@wsunix.wsu.edu> NNTP-Posting-Host: net.bio.net Art's Biotechnology Resource ---------------------------- The website can be linked by the following: http://biotech.isCool.net or http://www.ahpcc.unm.edu/~aroberts or http://www.arc.unm.edu/~aroberts This site allows easy access to hyperlinks and free software for the biochemist, biophysicist and molecular biologist. This site is constantly evolving and expanding, so it can be easy to use, reliable, and comprehensive. As of 6/13/99, many new links have been added. There have also been some new categories added: Employment Opportunities: this is a list of the "searchable" databases with jobs that are related to the biotechnology field. If you know of any links that are related to employment, please email me at arthurr@wsunix.wsu.edu Best Biotechnology Sites: this is a list of the best biotechnology- related sites in the world. If you know of any websites that are not on the list that would be considered the best, please email me at arthurr@wsunix.wsu.edu Bioethics/ Legal Issues: provides information on the public's view of biotechnology research and legal issues that concern the biotechnology community. If you know of any other important sites related to the legality of biotechnology or ethics (i.e. human cloning), please email me at arthurr@wsunix.wsu Sincerely, Art Roberts (web designer) arthurr@wsunix.wsu.edu (P.S. I reply to all emails that are sent, and I appreciate your comments and suggestions) From owner-proteins@net.bio.net Mon Jun 14 13:06:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!solaris.cc.vt.edu!news.vt.edu!portal.gmu.edu!news From: Debbie Grippaudo Newsgroups: bionet.molbio.proteins Subject: ATCC Biotech Patent & Licensing Forum Date: Mon, 14 Jun 1999 16:54:20 -0400 Organization: George Mason University, Fairfax, Virginia, USA Lines: 90 Message-ID: <37656BFB.6C6FCFEF@ib3.gmu.edu> NNTP-Posting-Host: 129.174.206.133 Mime-Version: 1.0 Content-Type: multipart/alternative; boundary="------------F1B3D2CCE28D2303436486F7" X-Mailer: Mozilla 4.5 (Macintosh; I; PPC) X-Accept-Language: en --------------F1B3D2CCE28D2303436486F7 Content-Type: text/plain; charset=us-ascii; x-mac-type="54455854"; x-mac-creator="4D4F5353" Content-Transfer-Encoding: 7bit 17th Annual ATCC Biotech Patent & Licensing Forum September 23 -26, 1999 Hyatt Dulles Hotel - Herndon, Virginia The American Type Culture Collection (ATCC) and The Institute for Biosciences, Bioinformatics and Biotechnology(IB3) at George Mason University, are proud to host the above conference. Please refer to our WEB site at URL: http://www.ib3.gmu.edu (follow the link to Conferences and Forums) for information on the meeting being held September 23 -16 , 1999. Following are just a few of the distinguished speakers who'll be presenting at this cutting-edge conference: Maria Freire - NIH Thomas Caskey - Merck Pharmaceuticals Joan Leonard - Howard Hughes Medical Institute Ian Pike - MRC, London Karen Hersey - MIT Jorge Goldstein - Stern, Kessler Should you have any questions or need additional information, please contact our Conference Coordinator: Deborah Grippaudo IB3 - George Mason University 10900 University Drive, MSN 4E3 Prince William Campus Manassas, VA 20110 703-993-8449 703-993-8460 (fax) email: debbieg@ib3.gmu.edu --------------F1B3D2CCE28D2303436486F7 Content-Type: text/html; charset=us-ascii Content-Transfer-Encoding: 7bit

17th Annual ATCC Biotech Patent & Licensing Forum

September 23 -26, 1999

Hyatt Dulles Hotel - Herndon, Virginia


The American Type Culture Collection (ATCC) and The Institute for Biosciences, Bioinformatics and Biotechnology(IB3) at George Mason University,  are proud to host the above conference.

Please refer to our WEB site at URL: http://www.ib3.gmu.edu (follow the link to Conferences and Forums) for information on the meeting being held September 23 -16 , 1999.  Following are just a few of the distinguished speakers who'll be presenting at this cutting-edge conference:

Maria Freire - NIH
Thomas Caskey - Merck Pharmaceuticals
Joan Leonard - Howard Hughes Medical Institute
Ian Pike - MRC, London
Karen Hersey - MIT
Jorge Goldstein - Stern, Kessler
 
 
 

Should you have any questions or need additional information,  please contact our Conference Coordinator:

Deborah Grippaudo
IB3 - George Mason University
10900 University Drive, MSN 4E3
Prince William Campus
Manassas, VA  20110
703-993-8449
703-993-8460 (fax)
email:  debbieg@ib3.gmu.edu
  --------------F1B3D2CCE28D2303436486F7-- From owner-proteins@net.bio.net Mon Jun 14 22:23:00 1999 Newsgroups: alt.support.cancer,bionet.molbio.gene-linkage,bionet.molbio.proteins Path: biosci!news.stanford.edu!newsfeed.stanford.edu!remarQ73!supernews.com!remarQ.com!dispose.news.demon.net!demon!newspeer.clara.net!news.clara.net!newsfeed.nacamar.de!newsfeed.tli.de!do.de.uu.net!uunet!ams.uu.net!ffx.uu.net!world!sphinx From: sphinx@world.std.com (SPHINX Technologies) Subject: Re: Your cancer cure! Message-ID: Date: Tue, 15 Jun 1999 06:16:37 GMT Bcc: sphinx References: <37616cf1.109178972@news.mindspring.com> <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net> Organization: SPHINX Technologies, Inc., Wellesley Hills, MA Lines: 52 Xref: biosci bionet.molbio.gene-linkage:2087 bionet.molbio.proteins:14464 Hah! We got a LIVE one! Thanks very much for your knowledgeable comments! In article , Peter wrote: > >... > >I think it is important at this point to define what makes a cell >cancerous. A cancer cell is a cell who has mutated genomic DNA. In order >for the cancer to destroy the organism, it must learn many new tricks. It >must learn how to live move, it must learn how to eat through basement >membranes, it must learn how to induce vasculatature, it must learn how to >move into the vasculature, it must learn how to survive in the blood, it >must learn how to get out of the vasculature and finally it must learn how >to live and grow in another site. All in all many genes need to be hit >genetically as to allow their in appropriate expression. I hope you are >realizing that cancer is a difficult thing to completly understand and it >is a very complex process. I do not believe that any one " magic bullet" >exists to cure all cancers. Most advanced cancers have very screwed up >DNA. If you looked at the chromasomes, you would see many breaks and >repairs and chromasome pieces may be located in inapropriate locations. >This is all very cursory explination, if you want more info, I would be >happy to direct to it. > I find your description of the cancerous cell very interesting. It reinforces my impression that cancer is not the result of randomly- altered genes, but is rather the result of purposeful manipulation of genes by some "purposeful" organism. As one with a certain level of knowledge of "combinatorics", or the art of mathematically counting complex things (and often using this to estimate probabilities or expected frequencies of occurrence), I find it very difficult to imagine how all the necessary FUNCTIONAL mutations to explain what you just described could have happened by chance in anything LIKE the current age of the universe. As you probably know, there is a small minority of researchers in the cancer research community who assert that there IS a cancer organism which they can isolate from any cancer cell and show you if you will only look. (Dr. Virginia Livingston-Wheeler was one of the better known.) Your description certainly sounds like the "trail" left by a purposeful organism, not chance alone! Thanks also for all the other detailed comments. It is going to take awhile for me to digest all the new information, which I very much appreciate. -John S. From owner-proteins@net.bio.net Tue Jun 15 05:07:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!howland.erols.net!portc02.blue.aol.com!pitt.edu!not-for-mail From: pxpst2@vms.cis.pitt.edu (Peter) Newsgroups: alt.support.cancer,bionet.molbio.gene-linkage,bionet.molbio.proteins Subject: Re: Your cancer cure! Date: Tue, 15 Jun 1999 09:01:14 -0400 Organization: University Of Pittsburgh Lines: 17 Message-ID: References: <37616cf1.109178972@news.mindspring.com> <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net> NNTP-Posting-Host: pelli.pathology.pitt.edu Mail-Copies-To: pxpst2@vms.cis.pitt.edu X-Newsreader: MT-NewsWatcher 2.4.4 Xref: biosci bionet.molbio.gene-linkage:2091 bionet.molbio.proteins:14467 In article , sphinx@world.std.com (SPHINX Technologies) wrote: > I find your description of the cancerous cell very interesting. It > reinforces my impression that cancer is not the result of randomly- > altered genes, but is rather the result of purposeful manipulation > of genes by some "purposeful" organism. It hust appears "purposeful". The only genetic hits that are noticed are ones that give a cell some survival advantage over another cell. For example, the p53 gene which has the abilty to detect flaws in the DNA and is responsible for halting the cell cycle so that DNA can be repaired. If this gene is turned into a dominant negative mutant then one will accumulate mutations at a fast rate and more growth regulatory genes will get hit and so on and so on... Peter From owner-proteins@net.bio.net Tue Jun 15 05:29:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!sunqbc.risq.qc.ca!newsflash.concordia.ca!pitt.edu!not-for-mail From: pxpst2@vms.cis.pitt.edu (Peter) Newsgroups: alt.support.cancer,bionet.molbio.gene-linkage,bionet.molbio.proteins Subject: Re: Your cancer cure! Date: Tue, 15 Jun 1999 09:22:29 -0400 Organization: University Of Pittsburgh Lines: 58 Message-ID: References: <37616cf1.109178972@news.mindspring.com> <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net> NNTP-Posting-Host: pelli.pathology.pitt.edu Mail-Copies-To: pxpst2@vms.cis.pitt.edu X-Newsreader: MT-NewsWatcher 2.4.4 Xref: biosci bionet.molbio.gene-linkage:2092 bionet.molbio.proteins:14468 In article , sphinx@world.std.com (SPHINX Technologies) wrote: > As one with a certain level of knowledge of "combinatorics", or the > art of mathematically counting complex things (and often using this > to estimate probabilities or expected frequencies of occurrence), I > find it very difficult to imagine how all the necessary FUNCTIONAL > mutations to explain what you just described could have happened > by chance in anything LIKE the current age of the universe. Why is it difficult? Keep in mind that mutations that do not allow for "selection" to occur are unnoticed and irrelevant. Also, you must bear in mind that certain genes are more important than others. As I mentioned earlier, the S phase (DNA sythesis phase) of the cell cycle is stoped by a protien called p53. If a mutaion occurs at the N17 ( I think that is the right place) then a dominant negative mutant will be created. And even though you may still have another good copy of p53 (from mom or dad), it will not work. Now the mutation rate will accelerate. And do not forget that the population of cells in the human is big (in the order of 10e8-10e9 cells). If one cell gets an advantage, then it will out grow its neighbors and increase the odds of another hit. Cancer researchers classify these growth genes as proto oncogenes (when normal) and oncogenes (when abnormal) and they can either be tumor suppressor genes(inhibit growth of normal cells) or tumor promoter genes(promote growth of normal cells). > > As you probably know, there is a small minority of researchers in > the cancer research community who assert that there IS a cancer > organism which they can isolate from any cancer cell and show you > if you will only look. (Dr. Virginia Livingston-Wheeler was one of > the better known.) That is complete and utter bullshit(pardon the english). It is known that virus can promote cancer. And there is some belief that chronic infections can possibly lead to cancer But the thought that an organism is the cause of Cancer is total garbage. What is interesting about the virus is that they have picked up small chunks of DNA that code for proteins that regulate the "growth genes I mentioned before. > > Your description certainly sounds like the "trail" left by a > purposeful organism, not chance alone! > > Thanks also for all the other detailed comments. It is going to take > awhile for me to digest all the new information, which I very much > appreciate. What I have given you is the present Dogma regarding Cancer. As a cancer researcher, I am comfortable with saying that all cancer researchers that I know believe that this is indeed the way Cancer works. The current dream is that methods to determine which of the protooncogenes have been turned to oncogenes and what drugs could be used to effect them. BTW, clonal expansion of cancer cells has been proven in rodents and humans. Regards, Peter Pediaditakis From owner-proteins@net.bio.net Tue Jun 15 06:34:00 1999 Path: biosci!agate!newsfeed.berkeley.edu!newsfeed1.swip.net!swipnet!news.algonet.se!newsfeed1.telenordia.se!algonet!newsfeed1.funet.fi!newsfeed.sunet.se!news01.sunet.se!news99.sunet.se!umdac!umu.se!not-for-mail From: Elisabeth Liu Newsgroups: bionet.molbio.proteins Subject: Help Date: Tue, 15 Jun 1999 16:20:57 -0700 Lines: 8 Message-ID: <3766DFD9.6F66@student.umu.se> NNTP-Posting-Host: pc1.climi.umu.se Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Trace: hudsucker.umdc.umu.se 929455996 798 130.239.180.153 (15 Jun 1999 14:13:16 GMT) X-Complaints-To: abuse@umu.se NNTP-Posting-Date: 15 Jun 1999 14:13:16 GMT X-Mailer: Mozilla 3.01 (Win95; I; 16bit) Hello, Does anyone know where to get vasoactive intestinal polypeptide receptor 2 (VIP2) antagonist and/or agonist? Thanks! Elisabeth Liu From owner-proteins@net.bio.net Tue Jun 15 07:00:00 1999 Path: biosci!news.stanford.edu!newsfeed.stanford.edu!newsfeed.berkeley.edu!newsfeed.tli.de!blackbush.xlink.net!news-kar1.dfn.de!news.embl-heidelberg.de!news.dkfz-heidelberg.de!news.urz.uni-heidelberg.de!genius.embnet.dkfz-heidelberg.de!un691cs From: CSC Newsgroups: alt.support.cancer,bionet.molbio.gene-linkage,bionet.molbio.proteins Subject: Re: Your cancer cure! Date: Tue, 15 Jun 1999 16:34:47 +0200 Organization: University of Heidelberg, Germany Lines: 61 Message-ID: References: <37616cf1.109178972@news.mindspring.com> <18650-3762C6C5-319@newsd-611.iap.bryant.webtv.net> NNTP-Posting-Host: genius.embnet.dkfz-heidelberg.de Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII In-Reply-To: Xref: biosci bionet.molbio.gene-linkage:2093 bionet.molbio.proteins:14470 On Tue, 15 Jun 1999, Peter wrote: > In article , sphinx@world.std.com (SPHINX > Technologies) wrote: > > > As one with a certain level of knowledge of "combinatorics", or the > > art of mathematically counting complex things (and often using this > > to estimate probabilities or expected frequencies of occurrence), I > > find it very difficult to imagine how all the necessary FUNCTIONAL > > mutations to explain what you just described could have happened > > by chance in anything LIKE the c