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.
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.
|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|
|Jin, Yi; Hoxie, Reyal S; Street, Timothy O (2017) Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity. Protein Sci 26:1206-1213|
|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|
|Tetone, Larry E; Friedman, Larry J; Osborne, Melisa L et al. (2017) Dynamics of GreB-RNA polymerase interaction allow a proofreading accessory protein to patrol for transcription complexes needing rescue. Proc Natl Acad Sci U S A 114:E1081-E1090|
|Morehouse, Benjamin R; Kumar, Ramasamy P; Matos, Jason O et al. (2017) Functional and Structural Characterization of a (+)-Limonene Synthase from Citrus sinensis. Biochemistry 56:1706-1715|
|Kumar, Ramasamy P; Morehouse, Benjamin R; Fofana, Josiane et al. (2017) Structure and monomer/dimer equilibrium for the guanylyl cyclase domain of the optogenetics protein RhoGC. J Biol Chem 292:21578-21589|
|Lamarche, Lindsey B; Kumar, Ramasamy P; Trieu, Melissa M et al. (2017) Purification and Characterization of RhoPDE, a Retinylidene/Phosphodiesterase Fusion Protein and Potential Optogenetic Tool from the Choanoflagellate Salpingoeca rosetta. Biochemistry 56:5812-5822|
|Devine, Erin L; Theobald, Douglas L; Oprian, Daniel D (2016) Relocating the Active-Site Lysine in Rhodopsin: 2. Evolutionary Intermediates. Biochemistry 55:4864-70|
|van der Feltz, Clarisse; Pomeranz Krummel, Daniel (2016) Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method. J Vis Exp :|
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