Document Detail


Coupled motion in proteins revealed by pressure perturbation.
MedLine Citation:
PMID:  22452540     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The cooperative nature of protein substructure and internal motion is a critical aspect of their functional competence about which little is known experimentally. NMR relaxation is used here to monitor the effects of high pressure on fast internal motion in the protein ubiquitin. In contrast to the main chain, the motions of the methyl-bearing side chains have a large and variable pressure dependence. Within the core, this pressure sensitivity correlates with the magnitude of motion at ambient pressure. Spatial clustering of the dynamic response to applied hydrostatic pressure is also seen, indicating localized cooperativity of motion on the sub-nanosecond time scale and suggesting regions of variable compressibility. These and other features indicate that the native ensemble contains a significant fraction of members with characteristics ascribed to the recently postulated "dry molten globule". The accompanying variable side-chain conformational entropy helps complete our view of the thermodynamic architecture underlying protein stability, folding, and function.
Authors:
Yinan Fu; Vignesh Kasinath; Veronica R Moorman; Nathaniel V Nucci; Vincent J Hilser; A Joshua Wand
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-04-10
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  134     ISSN:  1520-5126     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-10-11     Completed Date:  2013-01-02     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8543-50     Citation Subset:  IM    
Affiliation:
Graduate Group in Biochemistry and Molecular Biophysics, Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, 19104, United States.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle
Entropy
Humans
Models, Molecular
Motion
Nuclear Magnetic Resonance, Biomolecular
Pressure
Protein Conformation
Protein Stability
Ubiquitin / chemistry*
Grant Support
ID/Acronym/Agency:
DK 39806/DK/NIDDK NIH HHS; R01 DK039806/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Ubiquitin
Comments/Corrections

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


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