Colloquium Details
Evolutionary perspectives on protein folding, structure, and thermodynamics
Author: | Richard Goldstein Department of Chemistry, Biophysics Research Division, University of Michigan |
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Date: | October 16, 2001 |
Time: | 15:30 |
Location: | 100 Willamette |
Note: Special Time and Place
Abstract
Proteins fold into their native-state conformations in milliseconds to seconds, ignoring theoretical estimates that this process should take many times the age of the universe. Much work is directed to understanding how proteins are so much smarter than theorists, who cannot even reliably predict what the final folded states will be. Proteins have one major advantage over theorists - proteins have been working on this problem for billions of years. We can consider different ways in which proteins may have evolved to solve the protein-folding problem. Using simple theoretical models, we can show how neutral evolution and population dynamics combined with the need to fold can explain many of the observed properties of proteins, including the way proteins fold, the distribution of observed protein structures, the marginal stability of proteins, and how the evolutionary robustness of protein structures co-exists with sequence plasticity.