From owner-structural-nmr@net.bio.net Mon Jun 08 23:00:00 1998 Path: biosci!biosci!not-for-mail From: David Gorenstein Newsgroups: bionet.structural-nmr Subject: P-31 NMR Symposia Date: 9 Jun 1998 09:26:59 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 42 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear Colleague: The ICPC Organizing Committees and the Cincinnati Section of the ACS invite you to participate in the XIVth INTERNATIONAL CONFERENCE on PHOSPHORUS CHEMISTRY (ICPC) July 12-17, 1998 in Cincinnati, Ohio. One of the special features of this meeting will be the breadth of NMR and other spectroscopic topics. 31P NMR sessions include conventional NMR, solid state, MRI, and biological applications. Three major sessions of note and their chairs are as follows: "31P NMR Spectroscopy: Computational and Interpretive Advances" (L. Quin); "Biological 31P NMR" (D. Gorenstein); and "Spectroscopic and Microscopic Techniques for Bone and Calcium Phosphate Minerals" (Y. Pan, B. Borah). Two poster sessions with numerous other analytical related presentations will also be a major part of the meeting. Visit our website for registration forms, updates, and the complete program including presenters and titles: http://www.usc.edu/dept/ chemistry/ICPC14/index.html Most other major aspects of phosphorus chemistry will also be represented including an emphasis on bio-medical and industrial applications. Traditional strengths of the meeting, such as organic and inorganic chemistry will be supplemented with sessions on stereo and coordination chemistry. Theoretical aspects will also be presented. Biomedical related topics will also include oligonucleotides, catalytic antibodies, bio-organic, bisphosphonates, osteoporosis and dental applications, and radiopharmaceuticals. Further industrial uses such as agricultural chemistry, flame retardant, and chelation effects will be covered. For Additional Information Please Contact the Chairman: Dr. F. H. Ebetino Procter & Gamble Pharmaceuticals P. O. Box 8006 Mason, Ohio 45040-8006 513 622 3630 513 622 1195 fax ebetino.fh@pg.com From owner-structural-nmr@net.bio.net Mon Jun 08 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Thor Serti Newsgroups: bionet.structural-nmr Subject: Cholesterol 13C-NMR assignment ??????? Date: 9 Jun 1998 10:40:22 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 12 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <357D699B.41F88C06@urbanet.ch> NNTP-Posting-Host: net.bio.net Does anyone know what are the relative positions of C-12 and C-16 in cholesterol? The molecule is actually cholesteryl benzoate and his spectrum and assignment is in JOC (1975) 1675, and the assignment is the same in JOC (1977) 3325 (not sure about the page), that is: C-12(39.8), C-16 (28.1). In JACS (1969) 7445, however they wrote the contrary and had some work to back their version. Can you help me with this one please if you know better? From owner-structural-nmr@net.bio.net Thu Jun 11 23:00:00 1998 Path: biosci!biosci!not-for-mail From: geoff kelly Newsgroups: bionet.structural-nmr Subject: Postdoc in Biological NMR (London) Date: 12 Jun 1998 09:39:04 -0700 Organization: Imperial College, London, UK Lines: 17 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <35814F88.167E@ic.ac.uk> NNTP-Posting-Host: net.bio.net Postdoctoral Position in Biological NMR Applications are invited for a postdoctoral position, which is available for three years, to investigate the structure and function of eukaryotic RNA polymerase subunits using NMR. The biological NMR facility at Imperial College incorporates a new four channel high field NMR spectrometer, a silicon graphics suite and protein production laboratory. Candidates should have practical experience in NMR spectroscopy and knowledge of applications to macromolecules. Applications, consisting of CV, publication list, and a synopsis of research interests should be sent to Dr. Stephen Matthews, Department of Biochemistry, Imperial College, South Kensington, London, SW7 2AY (tel 0171 594 5315) mailto:s.j.matthews@ic.ac.uk From owner-structural-nmr@net.bio.net Thu Jun 11 23:00:00 1998 Path: biosci!biosci!not-for-mail From: mastone@indiana.edu (Martin J. Stone) Newsgroups: bionet.structural-nmr Subject: Postdoctoral Position Available Date: 12 Jun 1998 14:50:28 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 35 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <199806122126.QAA06026@indiana.edu> NNTP-Posting-Host: net.bio.net ******************************************* PROTEIN NMR POSTDOCTORAL POSITION AVAILABLE ******************************************* A postdoctoral position in protein NMR spectroscopy is available immediately in Martin Stone's laboratory in the Department of Chemistry, Indiana University, Bloomington, Indiana. The successful candidate will perform NMR relaxation and dynamics studies on several proteins, and related structural and biochemical experiments, with the aim of understanding the relationships between protein dynamics, structure, and function. Several NMR samples are already available. Candidates should have experience in protein NMR spectroscopy. Experience in protein expression and purification, enzymology, and computational chemistry would also be advantageous. In addition to a fully equipped biochemistry/molecular biology lab, we have the majority of time on a Varian UnityINOVA 500 MHz NMR spectrometer, equipped with triple resonance probes and 3-axis gradients. We also have several Silicon Graphics workstations with Biosym software. Bloomington is located in rolling hills about 50 miles south of Indianapolis. The area offers a wide range of outdoor activities and a rich cultural environment including Indiana University's world-famous School of Music. To apply, please send curriculum vitae, cover letter, and names and addresses (including telephone, fax, email) of at least two referees to: Prof. Martin J. Stone, Department of Chemistry, Indiana University, Bloomington, IN 47405-4001. Tel: (812) 855-6779 Fax: (812) 855-8300 email: mastone@indiana.edu From owner-structural-nmr@net.bio.net Thu Jun 11 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Jie Zheng Newsgroups: bionet.structural-nmr Subject: Biological NMR postdoctoral position Date: 12 Jun 1998 16:33:05 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 51 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <3581B22B.99D1EB30@rockvax.rockefeller.edu> Reply-To: zhengj@rockvax.rockefeller.edu NNTP-Posting-Host: net.bio.net --------------4399F522D7073ABF9025525D Content-Type: text/plain; charset=big5 Content-Transfer-Encoding: 7bit PROTEIN NMR POSTDOCTORAL POSITION AVAILABLE A biological NMR postdoctoral position is available immediately to study the structure and function of proteins involved in signal transduction at St. Jude Children's Research Hospital in Memphis, TN. The position is within the Department of Structure Biology which has outstanding facilities for NMR (600 MHz 4 channel spectrometers with gradients), protein crystallography, computer graphics, protein purification/characterization, and molecular biology. Applicants should have experience in NMR spectroscopy and/or protein expression and purification. If Interested, please contact Jie Zheng by e-mail at zhengj@rockvax.rockefeller.edu. --------------4399F522D7073ABF9025525D Content-Type: text/html; charset=big5 Content-Transfer-Encoding: 7bit

PROTEIN NMR POSTDOCTORAL POSITION AVAILABLE
 

A biological NMR postdoctoral position is available immediately
to study the structure and function of proteins involved in signal
transduction at St. Jude Children's Research Hospital in Memphis,
TN.  The position is within the Department of Structure Biology
which has outstanding facilities for NMR (600 MHz 4 channel
spectrometers with gradients), protein crystallography, computer
graphics, protein purification/characterization, and molecular biology.
Applicants should have experience in NMR spectroscopy and/or protein
expression and purification.  If Interested, please contact Jie Zheng
by e-mail at zhengj@rockvax.rockefeller.edu.
  --------------4399F522D7073ABF9025525D-- From owner-structural-nmr@net.bio.net Thu Jun 11 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Lawrence McIntosh Newsgroups: bionet.structural-nmr Subject: Postdoctoral position in Biological NMR Date: 12 Jun 1998 11:39:21 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 110 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net (Sorry if this appears twice - I had problems reaching the e-mail site). POSTDOCTORAL POSITION in BIOLOGICAL NMR A postdoctoral position is available for NMR studies of proteins involved in signal transduction and the regulation of gene expression. The successful candidate should have a solid background in biological NMR spectroscopy, including the determination of macromolecular structures using multi-dimensional heteronuclear methods. Experience in basic biophysics, molecular biology, and/or protein chemistry is also advantageous. The University of British Columbia offers an excellent academic environment, as well as unlimited opportunities for outdoor persuits in and around the city of Vancouver. Additional information on my research program, and involvment in the Protein Engineering Network of Centres of Excellence, can be found via http://www.science.ubc.ca/~chem/brochure/mcintosh.html. Interested applicants should send a CV, along with the phone numbers/ email addresses of two or more people familar with their work. ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ Lawrence McIntosh 2146 Health Sciences Mall Departments of Biochemistry and Chemistry University of British Columbia Vancouver, BC, Canada V6T 1Z3 mcintosh@otter.biochem.ubc.ca ph: (604) 822-3341 fax: (604) 822-5227 http://www.biochem.ubc.ca/ ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ From biosci-request@net.bio.net Fri Jun 12 17:21:50 1998 Received: from mta5.nts.uci.edu (mta5.nts.uci.edu [255.255.255.255]) by hemebase.bio.uci.edu (8.8.8/) with ESMTP id RAA20860 for ; Fri, 12 Jun 1998 17:21:50 GMT Received: (from daemon@localhost) by mta5.nts.uci.edu (8.8.5/8.8.5) id KAA12572 for raman@hemebase.bio.uci.edu.xyzzy; Fri, 12 Jun 1998 10:18:11 -0700 (PDT) Received: (from daemon@localhost) by mta5.nts.uci.edu (8.8.5/8.8.5) id KAA12551 for craman@uci.edu.xyzzy; Fri, 12 Jun 1998 10:18:08 -0700 (PDT) Received: from net.bio.net (net.bio.net [198.94.52.98]) by mta5.nts.uci.edu (8.8.5/8.8.5) with SMTP id KAA12533 for ; Fri, 12 Jun 1998 10:18:05 -0700 (PDT) Received: from mail-relay.ubc.ca (mail-relay.ubc.ca [137.82.1.2]) by net.bio.net (8.6.12-r-beta/8.6.6) with ESMTP id KAA23888; Fri, 12 Jun 1998 10:23:52 -0700 Received: from wolf.biochem.ubc.ca (wolf.biochem.ubc.ca [137.82.133.14]) by mail-relay.ubc.ca [137.82.1.2] (8.8.8/8.8.8) with SMTP id KAA05907 for <@hub.ubc.ca:str-nmr@net.bio.net>; Fri, 12 Jun 1998 10:21:40 -0700 (PDT) Received: from otter.biochem.ubc.ca by wolf.biochem.ubc.ca via ESMTP (951211.SGI.8.6.12.PATCH1502/951211.SGI) for id KAA17739; Thu, 14 Mar 1996 10:09:31 -0800 Sender: mcintosh@otter.biochem.ubc.ca Message-ID: <314860DB.CD80FB6E@otter.biochem.ubc.ca> Date: Thu, 14 Mar 1996 10:09:31 -0800 From: Lawrence McIntosh X-Mailer: Mozilla 4.04 [en] (X11; U; IRIX 5.3 IP22) MIME-Version: 1.0 To: str-nmr@net.bio.net Subject: POSTDOCTORAL POSITION in BIOLOGICAL NMR at UBC Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Status: RO POSTDOCTORAL POSITION in BIOLOGICAL NMR A postdoctoral position is available for NMR studies of proteins involved in signal transduction and the regulation of gene expression. The successful candidate should have a solid background in biological NMR spectroscopy, including the determination of macromolecular structures using multi-dimensional heteronuclear methods. Experience in basic biophysics, molecular biology, and/or protein chemistry is also advantageous. The University of British Columbia offers an excellent academic environment, as well as unlimited opportunities for outdoor persuits in and around the city of Vancouver. Additional information on my research program, and involvment in the Protein Engineering Network of Centres of Excellence, can be found via http://www.science.ubc.ca/~chem/brochure/mcintosh.html. Interested applicants should send a CV, along with the phone numbers/ email addresses of two or more people familar with their work. ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ Lawrence McIntosh 2146 Health Sciences Mall Departments of Biochemistry and Chemistry University of British Columbia Vancouver, BC, Canada V6T 1Z3 mcintosh@otter.biochem.ubc.ca ph: (604) 822-3341 fax: (604) 822-5227 http://www.biochem.ubc.ca/ ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~ From owner-structural-nmr@net.bio.net Fri Jun 12 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Esfandiar RAFII Newsgroups: bionet.structural-nmr Subject: P31 Chemical Shifts Date: 13 Jun 1998 06:57:17 -0700 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 8 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <33A0F878.7E05@u3pic105.u-3mrs.fr> NNTP-Posting-Host: net.bio.net Please help me to find a table of P31 chemical shifts, particularly for trialkyl phosphites. E. Rafii Universiti d'Aix-Marseille. Avenue Escadrille Normandie-Niemen. 13397-Marseille Cedex 20 e-mail : rafii@spi-chim.u-3mrs.fr From owner-structural-nmr@net.bio.net Sat Jun 13 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Rasmus Storjohann Newsgroups: bionet.structural-nmr Subject: Acetate neighbour effect on Halpha chemical shift Date: 14 Jun 1998 10:06:37 -0700 Organization: Simon Fraser University Lines: 25 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: References: <33A0F878.7E05@u3pic105.u-3mrs.fr> NNTP-Posting-Host: net.bio.net Hi, all, I want to compare the alpha proton chemical shifts of two different peptides. The shorter of the two is terminated with an acetate at the N-terminus, so that the sequence is Ac-Lys-..... In the other one the Lys is preceeded by Leu and then 20-odd residues more. Does anybody have values I can use to correct the chemical shifts for this neighbour effect so that the chemical shifts of the Lys alpha protons in the two peptides are comparable, and I can use them to infer whether they adopt similar conformations or not. Thanks, Rasmus ____________________________________________________________________ __ Rasmus Storjohann / /\ Institute of Molecular Biology / / \ and Biochemistry / / /\ \ Simon Fraser University / / /\ \ \ Burnaby, British Columbia V5A 1S6 / /_/__\ \ \ e-mail: rstorjoh@sfu.ca /________\ \ \ Phone: (604) 291-5657 / 415-0575 \___________\/ FAX: (604) 291-3765 From owner-structural-nmr@net.bio.net Sun Jun 14 23:00:00 1998 Path: biosci!biosci!not-for-mail From: "WielandWillker" Newsgroups: bionet.structural-nmr Subject: Re: Cholesterol 13C-NMR assignment ??????? Date: 15 Jun 1998 08:03:03 -0700 Organization: Universitaet Bremen, Germany Lines: 17 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <6m2m4e$lvh$1@kohl.informatik.uni-bremen.de> References: <357D699B.41F88C06@urbanet.ch> NNTP-Posting-Host: net.bio.net Thor Serti schrieb in Nachricht <357D699B.41F88C06@urbanet.ch>... >Does anyone know what are the relative positions of C-12 and C-16 in >cholesterol? > >The molecule is actually cholesteryl benzoate and his spectrum and >assignment is in JOC (1975) 1675, and the assignment is the same in JOC >(1977) 3325 (not sure about the page), that is: C-12(39.8), C-16 (28.1). > >In JACS (1969) 7445, however they wrote the contrary and had some work >to back their version. C-12(39.8), C-16 (28.1). This is correct. From owner-structural-nmr@net.bio.net Wed Jun 17 23:00:00 1998 Path: biosci!biosci!not-for-mail From: Athan Kuliopulos Newsgroups: bionet.structural-nmr Subject: Two Signal Transduction Postdoc Positions-Boston Date: 18 Jun 1998 08:58:20 -0700 Organization: NEMC Lines: 60 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <35892B02.40B0B346@opal.tufts.edu> Reply-To: "Kuliopoulos@HemOnc"@NEMC.nemc.org NNTP-Posting-Host: net.bio.net Two Postdoctoral Positions Available Molecular Cardiology Research Institute Tufts University School of Medicine-NEMC Boston, MA We have an immediate opening for two Postdoctoral Fellows to work in the field of molecular signaling and peptide-protein recognition. The projects focus on the human thrombin receptor. The thrombin receptor is activated by thrombin cleavage of the receptor exodomain and exposure of an N-terminal tethered ligand that binds to the body of the receptor. Receptor activation precipitates complex signaling events culminating in platelet aggregation, wound healing, and cellular proliferation. Since chronic activation of the receptor may lead to coronary artery disease, stroke, and other vascular diseases, preventing thrombin receptor activation is of pharmacologic interest. 1) Macromolecular Structural Studies of the Resting and Activated States of Thrombin Receptor Extracellular Domains. NMR structural studies of the thrombin receptor exodomain in activated and resting forms are currently in progress and a preliminary structure has been generated for the activated exodomain. Future projects include solving the structure of the exodomain complexed with extracellular loops. Insight into the molecular interactions between the exodomain and the body of the receptor should provide leads for the development of novel anti-thrombin receptor agents in collaboration with a pharmaceutical company. The NMR facility is located in the Medical School Biochemistry Department and current instrumentation include a new Bruker 600 MHz and updated 500 MHz magnets along with several SGI workstations. Our lab has close collaborations with NMR spectroscopists who provide additional technical expertise. 2) Thrombin-Cell Surface Protein Interactions; Development of Cell Surface-Specific Anti-Thrombotic Agents. During coagulation, the physiologic concentration of thrombin exceeds that of its thrombin receptor substrate. Therefore, thrombin has a difficult task of discriminating among the various cell surface proteins to find the receptor and cleave it in the millisecond time range. We are interested in exploring this unusual mechanism of substrate-assisted domain cleavage by thrombin and using this information to develop a novel class of cell surface anti-thrombin agents. The laboratory is located within the Molecular Cardiology Research Institute, a modern, state-of-the-art facility with a staff of 40 investigators including technical support. Qualifications for this position are a Ph.D. degree. Candidates with training in NMR who would like to acquire expertise in molecular biology are encouraged to apply. Interested candidates should e-mail a description of their research interests, a CV, and names of three references to: Athan Kuliopulos, MD., Ph.D. Assistant Professor of Medicine and Biochemistry Molecular Cardiology Research Institute Tufts-NEMC Box 832 750 Washington Street Boston, MA 02111 617-636-8482 617-636-4833 (fax) akuliopu@opal.tufts.edu From owner-structural-nmr@net.bio.net Thu Jun 18 23:00:00 1998 Path: biosci!biosci!not-for-mail From: "Axel T. Brunger" Newsgroups: bionet.structural-nmr Subject: Crystallography & NMR System: A New Program for Structure Determination Date: 19 Jun 1998 11:19:37 -0700 Organization: Howard Hughes Medical Institute Lines: 59 Sender: daemon@net.bio.net Approved: raman@hemebase.bio.uci.edu Distribution: world Message-ID: <358A9E09.31DF@laplace.csb.yale.edu> NNTP-Posting-Host: net.bio.net Development of a New Program For Structure Determination: Crystallography & NMR System Two years ago, development was started on a new program for structure determination called Crystallography & NMR System. This program is the result of an international collaborative effort among several research groups. The program has been designed to provide a flexible multi-level hierachical approach for the most commonly used algorithms in macromolecular structure determination. Highlights include heavy atom searching, experimental phasing (including MAD and MIR), density modification, crystallographic refinement with maximum likelihood targets, and NMR structure calculation using NOEs, J-coupling, chemical shift, and dipolar coupling data. The program is currently undergoing extensive beta-testing in a number of laboratories worldwide. We plan a general release in the Fall of 1998. A paper describing the philosophy of the program will soon be published in Acta Crystallographica D. Crystallography & NMR System will be made available to both academic and commercial users. The program will be provided to academic users with a small adminstrative fee and to commercial users through a yearly licensing scheme which will support a non-profit support and development group. This non-profit support and development group, headed by Dr. Paul Adams, has already been initiated at Yale University. Other members of the group currently include Dr. Ralf Grosse-Kunstleve. It is expected that other positions will be added later. As a consequence of this development, Dr. Brunger's group has terminated all development and support of the program X-PLOR. There is no active relationship between Dr. Brunger's group and Molecular Simulations Incorporated and no future relationship is planned. Announcement of the official release of Crystallography & NMR System will be made on the Internet as soon as it is available. Signed: Axel T. Brunger Professor of Molecular Biophysics and Biochemistry Investigator, Howard Hughes Medical Institute Principal Members of the Collaborative CNS effort: Dr. Marius Clore, National Institutes of Health Dr. Piet Gros, Utrecht University Dr. Michael Nilges, EMBL Heidelberg Dr. Randy Read, Cambridge University -- ======================================================================= | Axel T. Brunger Dept. Molecular Biophysics and Biochemistry| | Professor/Investigator Bass Center, 266 Whitney Avenue | | Office: 203-432-6143 Howard Hughes Medical Institute/Yale Univ. | | FAX: 203-432-6946 New Haven, CT 06520, USA. | | http://atb.csb.yale.edu | | mailto:brunger@laplace.csb.yale.edu | =======================================================================