Funding is requested for continued support of an interdisciplinary training program in molecular biophysics at Rutgers University. The program offers broad exposure to the experimental and theoretical techniques needed to solve problems in molecular biophysics together with in-depth training with a specific research problem. The graduate faculty of Rutgers University includes one of the largest and most active groups of molecular biophysicists in the country with interests ranging from molecular and submolecular problems to aspects of cellular organization and intact organisms. The training faculty are spread over four graduate programs at Rutgers and seven departments at Rutgers and the adjacent Robert Wood Johnson Medical School (formerly Rutgers Medical School) of the University of Medicine and Dentistry of New Jersey. There are significant research programs in X-ray crystallography and diffraction (Edward Arnold, Helen M. Berman, Barbara M. Brodsky, Millie M. Georgiadis, Ann Stock), nuclear magnetic resonance (Jean S. Baum, Gaetano T. Montelione), theoretical methods (Karsten Krogh- Jesperson, Ronald M. Levy, Gerald S. Manning, Wilma K. Olson), artificial intelligence (Casimir A. Kulikowski, Martin Farach), continuum mechanics (Bernard D. Coleman), biothermodynamics and spectroscopy (Kenneth J. Breslauer, Jeehiun K. Lee. Richard Ludescher, Tariq M. Rana, T.J. Thomas), electron microscopy (Donald A. Winkelmann), and biochemical synthesis and design (Stephen Anderson, Richard H. Ebright, Marc R. Gartenberg, Sarah E. Hitchcock-Dregregori, Masayori Inouye, Stephen S. Isied, Roger A. Jones, John W. Taylor). The faculty are a closely knit group with common interests in macromolecular structure, function, and interactions and with a history of fruitful interactions. Prospective trainees enter with undergraduate degrees in biology, chemistry, computer science, engineering, mathematics and physics. The program entails formal graduate courses, laboratory rotations, seminars, and dissertation research. Research groups are well equipped and well supported from extramural sources. The senior faculty have extensive experience in training students and the junior faculty are among the most promising young scientists in the nation. The intellectual climate is excellent and conducive to nurturing future research opportunities. Rutgers University and the University of Medicine of Dentistry have outstanding computational, imaging, NMR, and X-ray facilities available for training in molecular biophysics. The universities, together with the New Jersey Commission on Science and Technology, also jointly sponsor the New Jersey Center for Advanced Biotechnology and Medicine which has a strong research focus in molecular biophysics. The training program not only helps to meet national needs for personnel trained to apply the tools and concepts of the physical sciences to the solution of significant biological problems but also helps to enhance the academic environment within Rutgers University. The requested funds help to attract a pool of outstanding predoctoral students, to unify existing graduate offerings, and to offer an independent graduate curriculum in molecular biophysics.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM008319-12
Application #
6150871
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Program Officer
Flicker, Paula F
Project Start
1989-07-01
Project End
2004-06-30
Budget Start
2000-07-01
Budget End
2001-06-30
Support Year
12
Fiscal Year
2000
Total Cost
$148,409
Indirect Cost
Name
Rutgers University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
038633251
City
New Brunswick
State
NJ
Country
United States
Zip Code
08901
Balasubramanian, Sreekala; Xu, Fei; Olson, Wilma K (2009) DNA sequence-directed organization of chromatin: structure-based computational analysis of nucleosome-binding sequences. Biophys J 96:2245-60
Locasale, Jason W; Napoli, Andrew A; Chen, Shengfeng et al. (2009) Signatures of protein-DNA recognition in free DNA binding sites. J Mol Biol 386:1054-65
Barbieri, Christopher M; Kaul, Malvika; Pilch, Daniel S (2007) Use of 2-aminopurine as a fluorescent tool for characterizing antibiotic recognition of the bacterial rRNA A-site. Tetrahedron 63:3567-6574
Kaul, Malvika; Barbieri, Christopher M; Srinivasan, Annankoil R et al. (2007) Molecular determinants of antibiotic recognition and resistance by aminoglycoside phosphotransferase (3')-IIIa: a calorimetric and mutational analysis. J Mol Biol 369:142-56
Barbieri, Christopher M; Kaul, Malvika; Bozza-Hingos, Melanie et al. (2007) Defining the molecular forces that determine the impact of neomycin on bacterial protein synthesis: importance of the 2'-amino functionality. Antimicrob Agents Chemother 51:1760-9
Barbieri, Christopher M; Pilch, Daniel S (2006) Complete thermodynamic characterization of the multiple protonation equilibria of the aminoglycoside antibiotic paromomycin: a calorimetric and natural abundance 15N NMR study. Biophys J 90:1338-49
Hyde, Timothy J; Bryan, Michael A; Brodsky, Barbara et al. (2006) Sequence dependence of renucleation after a Gly mutation in model collagen peptides. J Biol Chem 281:36937-43
Togneri, John; Cheng, Yi-Shan; Munson, Mary et al. (2006) Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p. Proc Natl Acad Sci U S A 103:17730-5
Toro-Roman, Alejandro; Mack, Timothy R; Stock, Ann M (2005) Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face. J Mol Biol 349:11-26
Kaul, Malvika; Barbieri, Christopher M; Pilch, Daniel S (2005) Defining the basis for the specificity of aminoglycoside-rRNA recognition: a comparative study of drug binding to the A sites of Escherichia coli and human rRNA. J Mol Biol 346:119-34

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