The goal of this Training Program is to provide graduate students with advanced education in fundamental aspects of macromolecular chemistry, structure and mechanism. The program focuses on the basic physical-chemical and structural principles that give biological macromolecules their huge versatility of action in the living cell. The Training Program provides support for graduate students enrolled in two graduate programs here: Biochemistry, a highly structured program drawing students mainly from chemistry backgrounds, and Biophysics & Structural Biology, a relatively unstructured program for students from diverse quantitative undergraduate backgrounds. These two graduate programs, currently training a total of 59 students, operate within a larger group of four graduate programs in the life sciences. This Training Program involves 20 participating faculty from four university departments and provides training in the following areas: protein and nucleic acid structure determination by x-ray crystallography, cryo-electron microscopy, and magnetic resonance, mechanistic enzymology, single-molecule tracking analysis, catalytic RNA mechanisms, membrane protein structure and function, and mechanistic investigations of numerous specialized systems. All graduate students take a program of rigorous, quantitative courses and advanced research seminars, and all carry out 4 laboratory rotations in the first year. Students choose Ph.D. thesis advisors at the end of the first academic year m and typically proceed to the Ph.D. degree over the next four years. An overarching rationale of this program is that human disease must ultimately be understood in terms of the chemistry and physics of biological macromolecules.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM007596-26
Application #
6767806
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Program Officer
Flicker, Paula F
Project Start
1978-07-01
Project End
2007-06-30
Budget Start
2004-07-01
Budget End
2005-06-30
Support Year
26
Fiscal Year
2004
Total Cost
$260,855
Indirect Cost
Name
Brandeis University
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
02454
Turman, Daniel L; Cheloff, Abraham Z; Corrado, Alexis D et al. (2018) Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers. Biochemistry 57:1212-1218
Wirth, Jacob D; Boucher, Jeffrey I; Jacobowitz, Joseph R et al. (2018) Functional and Structural Resilience of the Active Site Loop in the Evolution of Plasmodium Lactate Dehydrogenase. Biochemistry 57:6434-6442
Wong, Nathan R; Liu, Xinyue; Lloyd, Hannah et al. (2018) A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild. J Inorg Biochem 188:96-101
Last, Nicholas B; Stockbridge, Randy B; Wilson, Ashley E et al. (2018) A CLC-type F-/H+ antiporter in ion-swapped conformations. Nat Struct Mol Biol 25:601-606
Pádua, Ricardo A P; Sun, Yizhi; Marko, Ingrid et al. (2018) Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2. Nat Commun 9:4507
Winterstein, Laura-Marie; Kukovetz, Kerri; Rauh, Oliver et al. (2018) Reconstitution and functional characterization of ion channels from nanodiscs in lipid bilayers. J Gen Physiol 150:637-646
Pochapsky, Thomas C; Wong, Nathan; Zhuang, Yihao et al. (2018) NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450. Biochim Biophys Acta Proteins Proteom 1866:126-133
Trieu, Melissa M; Devine, Erin L; Lamarche, Lindsey B et al. (2017) Expression, purification, and spectral tuning of RhoGC, a retinylidene/guanylyl cyclase fusion protein and optogenetics tool from the aquatic fungus Blastocladiella emersonii. J Biol Chem 292:10379-10389
Kumar, Ramasamy P; Morehouse, Benjamin R; Matos, Jason O et al. (2017) Structural Characterization of Early Michaelis Complexes in the Reaction Catalyzed by (+)-Limonene Synthase from Citrus sinensis Using Fluorinated Substrate Analogues. Biochemistry 56:1716-1725
Nguyen, Vy; Wilson, Christopher; Hoemberger, Marc et al. (2017) Evolutionary drivers of thermoadaptation in enzyme catalysis. Science 355:289-294

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