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MBRS - RISE at Fresno State |
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MBRS - RISE at Fresno State |
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Research Interests of Participating FacultyKrish Krishnan, Chemistry.Protein dynamics, folding, stability, and function are driven by non-covalent interactions. Native proteins at physiological temperatures continuously sample many conformations or conformational substrates. Prion diseases and other diseases of protein deposition provide some of the most compelling evidence for the importance of protein conformational dynamics and their impact on human health. Protein dynamics is also of considerable interest in the area of rationalized drug design. The proposed research will use an array of NMR-based experiments, with the support of biophysical theoretical tools including molecular dynamics simulations and computational approaches to develop new methods to understand molecular level mechanism of chemical and biological roles of proteins. The long-term objective of this research is to quantify the multiple time-scale dynamical information in proteins in a systematic fashion in order to establish a consensus definition of functional dynamics in proteins. Specific systems include (a) Characterize the dynamics of natively unfolded Phe-Gly rich nucleoporins, (b) Investigate the mechanism if freezing point depression of antifreeze glycoproteins (AFGPs), (c) Understand the molecular level details of transient states of amyloid initiation process and (d) Determine of role of hydration water in protein folding and stability. These projects involve extensive collaboration with Professors M.Rexach (Cell Biology, UCSC), Dr. M. Colvin (Natural Sciences, UC Merced), Y.Yeh (Applied Science, UC Davis), Y.Duan (Genome Center, UC Davis), W.H.Fink (Chemistry, UC Davis) and Dr. E. Lau (Biosciences, LLNL) |
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