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.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM007596-33
Application #
8496792
Study Section
Special Emphasis Panel (ZGM1-BRT-X (TG))
Program Officer
Flicker, Paula F
Project Start
1978-07-01
Project End
2014-06-30
Budget Start
2013-07-01
Budget End
2014-06-30
Support Year
33
Fiscal Year
2013
Total Cost
$231,942
Indirect Cost
$12,735
Name
Brandeis University
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
02454
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
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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
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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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