Document Detail

Protein stability at negative pressure.
MedLine Citation:
PMID:  20433926     Owner:  NLM     Status:  MEDLINE    
We record proton NMR spectra of the protein ubiquitin at 1 atmosphere pressure and at negative pressures (under tension), under conditions where the native and denatured states are nearly equally populated. Analysis of the unique histidine aromatic resonance of ubiquitin shows that negative pressure destabilizes the protein, in accord with a quadratic free energy dependence on pressure and temperature previously suggested in the literature. Our molecular dynamics simulations at negative pressure agree with the experimental result. In addition, molecular dynamics predicts a turnaround of the folding free energy at very low pressure. An 'island of stability' may exist at very negative pressures, where the protein is likely to fold into low density fluctuations of the solvent.
Edgar Larios; Martin Gruebele
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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.     Date:  2010-04-28
Journal Detail:
Title:  Methods (San Diego, Calif.)     Volume:  52     ISSN:  1095-9130     ISO Abbreviation:  Methods     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-09-06     Completed Date:  2010-12-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9426302     Medline TA:  Methods     Country:  United States    
Other Details:
Languages:  eng     Pagination:  51-6     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2010 Elsevier Inc. All rights reserved.
Department of Physics, University of Illinois at Urbana-Champaign, IL 61801, USA.
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MeSH Terms
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular
Protein Denaturation*
Protein Stability*
Protein Unfolding
Proteins / chemistry
Ubiquitin / chemistry
Reg. No./Substance:
0/Proteins; 0/Ubiquitin

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