Document Detail

Unifying microscopic mechanism for pressure and cold denaturations of proteins.
MedLine Citation:
PMID:  23006112     Owner:  NLM     Status:  In-Data-Review    
We study the stability of globular proteins as a function of temperature and pressure through NPT simulations of a coarse-grained model. We reproduce the elliptical stability of proteins and highlight a unifying microscopic mechanism for pressure and cold denaturations. The mechanism involves the solvation of nonpolar residues with a thin layer of water. These solvated states have lower volume and lower hydrogen-bond energy compared to other conformations of nonpolar solutes. Hence, these solvated states are favorable at high pressure and low temperature, and they facilitate protein unfolding under these thermodynamical conditions.
Cristiano L Dias
Publication Detail:
Type:  Journal Article     Date:  2012-07-27
Journal Detail:
Title:  Physical review letters     Volume:  109     ISSN:  1079-7114     ISO Abbreviation:  Phys. Rev. Lett.     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-09-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0401141     Medline TA:  Phys Rev Lett     Country:  United States    
Other Details:
Languages:  eng     Pagination:  048104     Citation Subset:  IM    
Fachbereich Physik, Freie Universität Berlin, Arnimalle 14, 14195 Berlin, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  Functional strain-line pattern in the human left ventricle.
Next Document:  Quantifying screening ion excesses in single-molecule force-extension experiments.