Home : Research : Principles of Protein Structure & Dynamics
Principles of Protein Structure & Dynamics
Structural biology is undergoing a quiet revolution. Despite the thousands
of high resolution – but static – protein structures now available
in the Protein Data Bank, scientists have broadly recognized that
many biochemical questions about these proteins remain open. The
reason is simple. By and large, proteins are machines that perform
their jobs by moving – rendering
a static view incomplete. Using both experimental and computational
approaches, a number of the training faculty have turned their attention
to the study of fluctuations and dynamics in biomolecules. Techniques include
NMR, Raman spectroscopy, coarse-grained computational modeling and other advanced
molecular simulation approaches.
Participating Faculty in this Area:
- Sanford Asher, Protein folding, structure & dynamics by Raman spectroscopy
- Ivet Bahar, Modeling and simulations of biomolecular dynamics
- Angela Gronenborn, Structural basis of signaling & gene regulations
- Chien Ho, NMR studies of allosteric proteins
- Hagai Meirovitch, Protein structure analysis
- Judith Klein-Seetharaman , Mapping
of sequence to structure, dynamics and function of proteins
- Daniel Zuckerman, Molecular dynamics & coarse-grained simulations
- Pei Tang, NMR & computations of protein structures,
dynamics & drug effects
- Maria Kurnikova, Molecular dynamics & function of channels
- Robert Swendsen, Computer simulations of biological molecules
- John Rosenberg, DNA recognition by X-ray & statistical mechanics
- Rob Coalson, Theory of chemical dynamics
- Joanne Yeh, Membrane Proteins Fold and Conformation via X-ray
Crystallography; Computational Studies of Membrane Translocation and Insertion
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