This Training Program provides graduate students with advanced education in the principles and practice of macromolecular chemistry, mechanism, and structure. All aspects of the program - formal course curriculum, laboratory rotations, informal specialized area-interest seminars, and intensive research in laboratories operating on the edge of discovery - are aimed at the question: how do biological macromolecules work? How do proteins, membranes, nucleic acids, and high-order complexes of these huge molecules use physical-chemical and structural principles to act in the enormous variety of contexts that underlie biological function? The Training Program provides support for selected graduate students in two of the four life-science graduate Ph.D. programs at Brandeis: Biochemistry, and Biophysics &Structural Biology. The former of these is a more structured program that attracts students mainly with strong academic backgrounds in chemistry and biochemistry backgrounds, while the latter is a more flexible program designed for students who have strong quantitative backgrounds but who may have weaker prior training experience in biological chemistry. Our intention is to bring these two groups of students to the same end-point and to prepare them for careers in basic research. Currently, 28 students (which will rise to 33 students in September 08) are enrolled in these two Ph.D. programs;the Training Program includes 20 participating faculty (in four departments) working in the following areas: macromolecular structure determination by x-ray crystallography and NMR, mechanistic enzymology, membrane transport and ion channel mechanisms, single-molecule analysis, high-resolution mass spectroscopy and proteomics, computational biophysics.

Public Health Relevance

A general rationale for the value of this program is the conviction that human disease must ultimately be understood in terms of the chemistry and physics of biological macromolecules.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Institutional National Research Service Award (T32)
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Special Emphasis Panel (ZGM1-BRT-X (TG))
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Flicker, Paula F
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Brandeis University
Schools of Arts and Sciences
United States
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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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