Document Detail

Missense meanderings in sequence space: a biophysical view of protein evolution.
MedLine Citation:
PMID:  16074985     Owner:  NLM     Status:  MEDLINE    
Proteins are finicky molecules; they are barely stable and are prone to aggregate, but they must function in a crowded environment that is full of degradative enzymes bent on their destruction. It is no surprise that many common diseases are due to missense mutations that affect protein stability and aggregation. Here we review the literature on biophysics as it relates to molecular evolution, focusing on how protein stability and aggregation affect organismal fitness. We then advance a biophysical model of protein evolution that helps us to understand phenomena that range from the dynamics of molecular adaptation to the clock-like rate of protein evolution.
Mark A DePristo; Daniel M Weinreich; Daniel L Hartl
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review    
Journal Detail:
Title:  Nature reviews. Genetics     Volume:  6     ISSN:  1471-0056     ISO Abbreviation:  Nat. Rev. Genet.     Publication Date:  2005 Sep 
Date Detail:
Created Date:  2005-09-09     Completed Date:  2006-01-05     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  100962779     Medline TA:  Nat Rev Genet     Country:  England    
Other Details:
Languages:  eng     Pagination:  678-87     Citation Subset:  IM    
Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
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MeSH Terms
Adaptation, Biological / genetics*
Biophysical Phenomena
DNA / genetics*
Evolution, Molecular*
Models, Genetic*
Mutation, Missense / genetics*
Protein Conformation
Protein Folding
Proteins / genetics*,  metabolism
Selection, Genetic
Reg. No./Substance:
0/Proteins; 9007-49-2/DNA

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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