From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Sharon Campbell Newsgroups: bionet.structural-nmr Subject: Postdoctoral positions-biomolecular NMR Date: 19 Jan 1999 21:37:58 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 27 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <362DFAC8.7820@med.unc.edu> Reply-To: campbesl@med.unc.edu NNTP-Posting-Host: net.bio.net I=92d like to bring your attention to availability of one, possibly two postdoctoral positions in NMR structural biology. Research efforts in our laboratory are centered on the structure, biochemistry and biology of Ras, Ras-related proteins, and their regulatory factors. Ras and Rho family GTPases function as molecular switches that regulate a variety of signal transduction pathways leading to changes in cell growth, cell morphology and apoptosis. We are interested in elucidating how Ras (and Ras-related proteins) recognize regulatory proteins and downstream targets(s), and how these interactions modulate the signal transmission process. The laboratory is equipped with several SGI workstations, a host of software packages for processing, analysis and biomolecular NMR structure determination (including Felix and NMR Refine), a wet biochemistry laboratory and 4 channel Varian Inova 500 and 600 MHz spectrometers. =20 Interested candidates should send their CV by email or fax to campbesl@med.unc.edu. These positions are fully funded for two to three years. Sharon Campbell Assistant Professor Department of Biochemistry and Biophysics U. of North Carolina Chapel Hill, NC 27599-7260 From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Lawrence McIntosh Newsgroups: bionet.structural-nmr Subject: Biophysics Grad. Program Date: 19 Jan 1999 21:46:03 -0800 Organization: ubc Lines: 27 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <368ECC71.2E9205B4@otter.biochem.ubc.ca> Reply-To: mcintosh@otter.biochem.ubc.ca NNTP-Posting-Host: net.bio.net --------------196FB2F15CEFDD33D6078A67 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit Hello: We are beginning to organize a graduate program in molecular biophysics / structural biology at the University of British Columbia. The program will likely bridge numerous departments / faculties and involve a common series of graduate level courses and seminars. If you are involved in a similar program, or know of one, I would greatly appreciate any information (e.g. brochures, websites) or practical advice describing its organization, requirements, courses, etc. With thanks, Lawrence McIntosh Department of Biochemistry 2146 Health Sciences Mall University of British Columbia Vancouver, BC, Canada V6T 1Z3 mcintosh@otter.biochem.ubc.ca From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Sarata C Sahu Newsgroups: bionet.structural-nmr Subject: folding problem in NMR Date: 19 Jan 1999 21:49:08 -0800 Organization: Tata Institute of Fundamental Research Lines: 8 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <3660B6ED.41C6@tifr.res.in> NNTP-Posting-Host: net.bio.net While recording a 15N-NOESY_HSQC, the spectra got folded by ~1.4 PPM along 15N dimension. Since it is difficult to repeat the experiment (you know how hard it is to get NMR time...anywhere!) I was wondering whether anyone has some felix macro to overcome this problem. Thankx sarata From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Krishna Rajarathnam Newsgroups: bionet.structural-nmr Subject: Re:postdoctoral positions in NMR Date: 19 Jan 1999 21:48:23 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 19 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <3665AE28.18B690BD@hbcg.utmb.edu> NNTP-Posting-Host: net.bio.net POSTDOCTORAL positions available immediately to study proteins and protein-receptor complexes involved in a variety of immune related diseases using NMR spectroscopy. Preference given to candidates with prior experience in biological NMR but individuals with a strong interest in protein NMR and trained in molecular biology and protein chemistry, computational chemistry or biophysical chemistry will also be considered. Excellent facilities are available including 4 channel 750 and 600 MHz Varian spectrometers, workstations, and resources for protein expression and purification. UTMB structural biology group involves investigators in NMR, X-ray, computational, and biophysical techniques and offers a stimulating scientific environment. Salary commensurate with experience. Email responses are encouraged. Please send a CV and names of two references to: Dr. Krishna Rajarathnam Dept. Human Biological Chemistry and Genetics 5.138 Medical Research Building University of Texas Medical Branch Galveston, TX 77555-1055. E-mail: krishna@hbcg.utmb.edu From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: rossa@rbaw01.bas.roche.com Newsgroups: bionet.structural-nmr Subject: Two lock solvents. Date: 19 Jan 1999 21:46:31 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 40 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <9812301405.ZM18426@sodium.bas.roche.com> Reply-To: alfred.ross@roche.com NNTP-Posting-Host: net.bio.net Dear NMR people, I have the following problem: In the samples (H2O/Protein) I have to use are two deuterated compounds (D2O, DMSO) of about the same (5%) concentration. When running the Bruker DRX spectrometer with a sample changer a automatic lock procedure is always performed for each sample. For this procedure a solvent can be selected (e.g. D2O). Now the BSMS lock system looks in the full possible sweep range of the device for the biggest signal and asumes this to be the selected lock compound (which is sometimes D2O and sometimes DMSO). If it selects now the DMSO signal to be the D2O signal watersupression fails completely for the succeeding experimen! My question: How can one define the sweep-amplitude of the lock-device if it is running under automated lock condtions? Is there another problem to circumvent the problem? As always: Thanks a lot for any comment and a happy new year from Alfred Ross -- ************************************* Dr. Alfred Ross NMR-Spectroscopist e-mail: alfred.ross@roche.com ******* Phone: CH-(0)61-6887029 * * Fax: CH-(0)61-6887408 * ROCHE * * * Mail: F. Hoffmann-LaRoche AG ******* (Dr. A. Ross - PRPC-S) Grenzacherstr. 124 CH-4070 Basel ************************************* Phone(private): D-(0)7621-49710 From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: "Hidekazu HIROAKI, PhD" Newsgroups: bionet.structural-nmr Subject: Anout CNS ? Date: 19 Jan 1999 21:42:47 -0800 Organization: Dept Str Biol, Biomolecular Engineering Reserach Institute, JAPAN Lines: 27 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <3694B203.2727@antispam.beri.co.jp> Reply-To: hiroakih@antispam.beri.co.jp NNTP-Posting-Host: net.bio.net Hi all, I'm now interested in the new program suite "CNS" developped by Brunger's group. I like to ask very stupid (but practical) question about CNS to someone who has experienced to compare the same NMR structure calculation project with different programs (dyana and/or XPLOR). Q1. In brief, what is the most advantage to use CNS rather than older version of XPLOR ? Q2. How faster (or heavier) CNS is ? Q3. Do we need higher computation power and resourses ? Thank you very much. hiroaki@antispam.beri.co.jp ------------------- Hidekazu HIROAKI, Dept of Structural Biology, Biomolecular Engineering Research Institute, Osaka, JAPAN ------------------- Remove 'antispam.' from my mail address before replying. ------------------- From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Istvan Pelczer Newsgroups: bionet.structural-nmr Subject: open positions Date: 19 Jan 1999 21:44:57 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 133 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear Colleagues, There are two open positions at Dept. of Chemistry, Princeton University. Please, find the ads below. Best regards, Istvan wwww,wwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwwww= wwww Istvan Pelczer, Ph.D. Email: ipelczer@princeton.edu Senior NMR Spectroscopist Princeton University Department of Chemistry, Frick Lab., ph# (609) 258 2342 Washington Road fax# (609) 258 6746 Princeton, NJ 08544, USA Book Review Editor for "The NMR Newsletter" http://www.nmrnewsletter.com * * * MAGNETIC RESONANCE SPECTROSCOPIST-PhD Professional Staff Position: Princeton University has an immediate opening for a Ph.D. level magnetic resonance spectroscopist with preferred experience in, e.g., EPR/ENDOR a= nd solid state NMR spectroscopy. Primary duties involve maintenance of related instrumentation (hardware) and associated peripherals, including all spectrometer components, workstations, cryostats, probes, cavities, resonators and plotters; special projects in hardware design, training o= f new users on basic as well as advanced techniques; scheduling and bookkeeping of multi-user instruments, educating students and faculty in new magnetic resonance methods and instructor for lectures on the theory= of instrument operation; drafting of instrumentation proposals. The spectroscopist will fill one of two Professional Staff positions with complementary skills and overlapping instrument responsibilities in a growing NMR/EPR facility (5 NMRs, 2 EPRs, 1 ENDOR). Send resume to: Pro= f. Charles Dismukes, Operations Committee, Dept. of Chemistry, Princeton University, Princeton, NJ 08544. Princeton University is an Equal Opportunity/Affirmative Action employer. * * * Pulsed-EPR/ENDOR Spectroscopist - Postdoctoral Research Scientist: =20 Princeton University has an immediate opening for a recent PhD scientist with experience in pulsed EPR spectroscopy and multiple resonance spectroscopy (ENDOR). Primary responsibilities include applications of these methods via collaborative internal projects with chemists and enzymologists in training (undergraduates, graduate students and postdoctoral scientists). An opportunity exists to learn about recent discoveries in a several areas of scientific research within inorganic chemistry, photochemistry, solar energy conversion, metallo-enzymes, biochemistry and photosynthesis via a collaborative approach. Available spectrometers includes Bruker ESP300E and Elexsys585 spectrometers. For examples of the types of problems consult the publications below or view the Internet webpage: http://www.princeton.edu/~catalase/ Send resume to: Prof. Charles Dismukes, Hoyt Laboratory, Dept. of Chemistry, Princet= on University, Princeton, NJ 08544. =20 W. Ruttinger And G. C. Dismukes, "Synthetic Water Oxidation Catalysts fo= r Artificial Photosynthetic Water Oxidation," Chemical Reviews, 97, 1-24 (1997). =20 Sossong, T.J., S.V. Khangulov, R.C. Cavalli, D.R. Soprano, G.C. Dismukes= , and D.E. Ash, "Catalysis on Dinuclear Mn(II) Centers: Hydrolytic and Red= ox Activities of Rat Liver Arginase." (1997). J. Bioinorganic Chemistry, 2, 433-443. =20 Zaltsman, L., E. Bruntrager, G. Ananyev, and G.C. Dismukes, "A Quantitat= ive Kinetic Model for Photo-assembly of the Photosynthetic Water Oxidase fro= m its Inorganic Constituents: Requirements for Manganese and Calcium in th= e Kinetically Resolved Steps."Biochemistry , 36, 8914-8922 (1997). =20 R=FCttinger, W., C. Campana, and G.C. Dismukes, "Synthesis and Characterization of a Mn4O4L6 Complex with Cubane-like Core Structure: A New Class of Models of the Active Site of the Photosynthesis Water Oxidase." J. Amer. Chem. Soc., 119, 6670-6671 (1997). =20 G. M. Ananyev and G. C. Dismukes, "Calcium Induces Binding and Formation= of a Spin-coupled Dimanganese (II,II) Center in the apo-Water Oxidation Complex of Photosystem II as Precursor to the Functional Tetra-Mn/Ca Cluster." Biochemistry, 36, 11342-11350 (1997). =20 S. V. Khangulov, T. M. Sossong, Jr., D. E. Ash, G. C. Dismukes, "L-argin= ine Binding to Liver Arginase Requires Proton Transfer to Gateway Residue His141 and Coordination of the Guanidinium Group to the Dimanganese(II,I= I) Center." Biochemistry, 37: p. 8539-8550 (1998) =20 Zheng, M., and Dismukes, G. C. "Resolution Enhancement in ENDOR Spectroscopy by Distant-Dependent Enhanced ENDOR Phase (DEEP) Spectrosco= py: Application to Determination of the Solvation Structure Around Paramagne= tic Ions in Disordered Solids" J. Physical Chemistry (B), 102, 8306-8313 (19= 98). =20 Dismukes, G.C., Ruettinger,W., Boelrijk, A.E.M., Ho, D., STRUCTURE OF TH= E Mn4Ca1 CORE OF THE PSII WATER OXIDIZING COMPLEX AND THE Mn4O4-CUBANE/ Mn4O2-BUTTERFLY MODEL COMPLEXES, in Proceedings XIth International Photosynthesis Congress, G. Garob, Editor. 1998, Kluwer Academic: Dordre= cht. =20 Ananyev, G.M., Zaltsman, L., McInturff, R.A. & Dismukes, G.C. (1998) "Assembly Intermediates and "Inorganic Mutants" of the PSII Oxygen Evolv= ing Complex" in Proceedings XIth International Photosynthesis Congress, G. Garob, Editor. 1998, Kluwer Academic: Dordrecht. =20 Khangulov, S.V., V.N. Gladyshev, G.C. Dismukes, and T.C. Stadtman, "Selenium Containing Formate Dehydrogenase H from E. Coli: A Molybdopter= in Enzyme that Catalyzes Formate Oxidation without Oxygen Transfer." Biochemistry, 1998. 37: p. 3518-3528. From owner-structural-nmr@net.bio.net Tue Jan 19 22:00:00 1999 Path: biosci!biosci!not-for-mail From: "Yoram A. Puius" Newsgroups: bionet.structural-nmr Subject: Postdoctoral Positions: Crystallography and NMR Date: 19 Jan 1999 21:41:00 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 25 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Two postdoctoral positions (one Protein Crystallographer and one NMR Spectroscopist) are immediately available for studying the structural basis of substrate/inhibitor specificity and structure/dynamics of protein tyrosine phosphatases (PTPases). This is a large family of enzymes that regulate a variety of signal transduction processes and are involved in a number of human diseases such as cancer and diabetes. Projects include: analysis of PTPase-substrate, PTPase-inhibitor, and mutant PTPases structures; investigation of the relationship between dynamics and PTPase catalysis; and design and synthesis of potent and selective nonpeptidic PTPase inhibitors. Candidates with experience in protein crystallography or NMR and want to extend their expertise to the other areas are encouraged to apply. Send curriculum vitae, names and telephone numbers of three references to: Dr. Zhong-Yin Zhang Department of Molecular Pharmacology Albert Einstein College of Medicine 1300 Morris Park Ave., Bronx, NY 10461 U.S.A. email: zyzhang@aecom.yu.edu From owner-structural-nmr@net.bio.net Thu Jan 21 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Tobin Sosnick Newsgroups: bionet.structural-nmr Subject: Post-doctoral position in protein folding Date: 22 Jan 1999 11:10:57 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 8 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <3.0.32.19990122122723.0160e06c@acs-popmail.uchicago.edu> NNTP-Posting-Host: net.bio.net POSTDOCTORAL POSITION IN PROTEIN FOLDING AND STABILITY AT UNIVERSITY OF CHICAGO. NIH funded position to conduct biophysical studies of folding, dynamics and function using NMR, mass spectrometry, hydrogen exchange, H/D isotope fractionation, and mutagenesis. Prior experience in NMR highly desirable but not necessary. Please send applications to Prof. Tobin Sosnick (trsosnic@midway.uchicago.edu), Dept. of Biochem. & Mol. Biol., 920 E. 58th St. Chicago, IL 60637. The University of Chicago is an AA/EO Employer From owner-structural-nmr@net.bio.net Fri Jan 22 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Chuck Sanders Newsgroups: bionet.structural-nmr Subject: NMR Facility Manager Date: 23 Jan 1999 10:04:57 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 29 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <36AA045B.F27BDE83@po.cwru.edu> NNTP-Posting-Host: net.bio.net Position Announcement: NMR Facility Manager- Cleveland Center for Structural Biology The Cleveland Center for Structural Biology (CCSB) has an immediate opening for the position of NMR Facility Manager. The main responsibilities include operation and maintenance of the state-of-the-art capabilities of five high field Varian INOVA spectrometers (three 600 MHz, one 500 MHz, one 300 MHz WB), and instruction of new and external operators. The CCSB is a collaborative enterprise involving Case Western Reserve University, the Cleveland Clinic Foundation, and Cleveland State University. Further expansion of the NMR facilities of the CCSB is expected, along with future additional NMR staff recruitment. Experience in all aspects of maintaining high field super-conducting magnets and operation of high field spectrometers is preferred. Effective verbal and written communication skills are essential. Please send a resume and names of three references to: John J. Mieyal, Ph.D. Professor of Pharmacology and Chemistry Director, Cleveland Center for Structural Biology Case Western Reserve University School of Medicine, Department of Pharmacology 10900 Euclid Avenue Cleveland, OH 44106-4965 Case Western Reserve University is an equal opportunity, affirmative action employer. From owner-structural-nmr@net.bio.net Mon Jan 25 22:00:00 1999 Path: biosci!biosci!not-for-mail From: porn@atc.atccu.chula.ac.th Newsgroups: bionet.structural-nmr Subject: help! NMR study of an enzyme Date: 26 Jan 1999 08:59:07 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 33 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear Sir I have conducted an NMR study of the enzyme dihydrofolate reductase (18 kDa) expressed from E. coli. At the present time, I could obtain about 1-2 mM of the pure enzyme in 0.6 ml sample solution. We (my co-workers) pushed a lot of efforts to increase the solubility without success. Meanwhile I initiated NMR investigation by acquiring a series of 1H 1D NMR spectra with various ligand concentrations to identify the exchange rate with its inhibitor added and to determine th e association constant in the formation of the enzyme-inhibitor complex. However the problem was that the binary complex was not stable. What I got was the precipitated sample at the bottom of the NMR tube. Therefore, the spectra are not reliable. Addition of 20% of deuterated glycerol into the solution could help a little bit but it still precipitated at the longer time. Recently, I have a stock containing about 90 mg of the lyophilized enzyme. Should I follow the same procedure? I would appreciate if anyone could kindly be of help or share your experiences. Is the road that we are going the right way? If yes. What should I do to overcome the problem and reach the objective proposed? Should I continue to use the glycerol and what I should play attention to the effect of glycerol? Any comments are welcome. BTW, I use 400 MHz NMR. But NMR resouces are very instrumentally limited. In particular, there is no temperature control unit for monitoring the temperature of the sample in the probe. This should be also play an attention, shouldn't it? Thank you for your time and I look forward to hear from your response. Thep From owner-structural-nmr@net.bio.net Tue Jan 26 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Paul Driscoll Newsgroups: bionet.structural-nmr Subject: Postdoctoral Fellowship/Biomol. NMR/UCL Date: 27 Jan 1999 12:09:22 -0800 Organization: Dept. Biochem. & Mol. Biol., UCL Lines: 49 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: <78nlfd$7u1$1@mserv2.dl.ac.uk> NNTP-Posting-Host: net.bio.net Postdoctoral Fellowship in Biomolecular NMR Spectroscopy -------------------------------------------------------- Department of Biochemistry and Molecular Biology, University College London A post-doctoral fellowship position is available in the Department of Biochemistry and Molecular Biology, University College London to work on the application of NMR to the structure-function characterisation of proteins. The project will involve integration of the NMR studies with the group's interests in thermodynamic investigations of protein-ligand binding interactions. The position is funded for two years by the B.B.S.R.C. The project will be jointly supervised by Drs. John Ladbury and Paul Driscoll. The applicant should have recently completed a Ph.D. in structural biology or related discipline and have experience of multi-dimensional NMR techniques applied to isotope-labelled proteins. The NMR group currently comprises 10 researchers at student to post-doctoral level, is well equipped for molecular biology, protein expression and purification, and NMR spectroscopy (three channel and four channel 600 and 500 MHz Varian spectrometers with pulse shaping and pulse field gradient accessories) and computing. We enjoy routine access to ultra-high-field NMR spectrometers operating at 800 MHz. We are a major component of the recently inaugurated Joint Research School (JRS) in Biomolecular Sciences set up in conjunction with the Department of Crystallography at Birkbeck College, headed by Professor Janet Thornton. The JRS has just been accorded the status of the 'Bloomsbury Structure Biology Centre' supported by a major award from the B.B.S.R.C. The salary for this position is in the range #17,590-#20,107 plus #2,134 London supplement, dependent on age and experience. The position is available immediately, however recent or prospective Ph.D. garduates are encouraged to apply. Contact Dr. John Ladbury (44-171 380 7012) for further details, if required. Applicants should mail or E-mail Dr. John Ladbury or Dr. Paul Driscoll, Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, U.K.; ladbury@biochem.ucl.ac.uk; driscoll@biochem.ucl.ac.uk) with a c.v. and the names and addresses of three referees by 1st March 1999. -- Dr. Paul C. Driscoll Snr. Lecturer, Joint UCL/LICR NMR Laboratory --------------------------------------------------------------------- Dr. Paul C. Driscoll | Office (answer)phone: (44)-171 380 7035 Dept. Biochem. & Mol. Biol. | Department fax: (44)-171 380 7193 University College London | driscoll@biochem.ucl.ac.uk From owner-structural-nmr@net.bio.net Thu Jan 28 22:00:00 1999 Path: biosci!biosci!not-for-mail From: Sylvie.Lucas@univ-rennes1.fr (Sylvie Lucas) Newsgroups: bionet.structural-nmr Subject: compatibility beetwen bruker x-winnmr and apple 8500 laserwriter Date: 29 Jan 1999 08:07:30 -0800 Organization: Universite de Rennes 1 Lines: 12 Sender: daemon@net.bio.net Approved: raman@bragg.bio.uci.edu Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net hello, i work on a 200 dpx nmr spectrometer using x-winnmr1.3 bruker sofware installed on a indy station ( irix 5.3 ) i want to know if the apple laserwriter 8500 is compatible with this configuration and if it's ok , which driver may i use ? with thanks jean-paul guegan phone : 02-99-28-62-82 univ rennes 1