Document Detail

Solvent mobility and the protein 'glass' transition.
MedLine Citation:
PMID:  10625424     Owner:  NLM     Status:  MEDLINE    
Proteins and other biomolecules undergo a dynamic transition near 200 K to a glass-like solid state with small atomic fluctuations. This dynamic transition can inhibit biological function. To provide a deeper understanding of the relative importance of solvent mobility and the intrinsic protein energy surface in the transition, a novel molecular dynamics simulation procedure with the protein and solvent at different temperatures has been used. Solvent mobility is shown to be the dominant factor in determining the atomic fluctuations above 180 K, although intrinsic protein effects become important at lower temperatures. The simulations thus complement experimental studies by demonstrating the essential role of solvent in controlling functionally important protein fluctuations.
D Vitkup; D Ringe; G A Petsko; M Karplus
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Nature structural biology     Volume:  7     ISSN:  1072-8368     ISO Abbreviation:  Nat. Struct. Biol.     Publication Date:  2000 Jan 
Date Detail:
Created Date:  2000-01-18     Completed Date:  2000-01-18     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9421566     Medline TA:  Nat Struct Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  34-8     Citation Subset:  IM    
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454-9110, USA.
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MeSH Terms
Computer Simulation*
Glass / chemistry
Hot Temperature
Myoglobin / chemistry*,  metabolism
Protein Structure, Secondary
Solvents / chemistry*,  metabolism
Water / metabolism
Reg. No./Substance:
0/Myoglobin; 0/Solvents; 0/carboxymyoglobin; 7732-18-5/Water

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

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