Document Detail


Epistructural tension promotes protein associations.
MedLine Citation:
PMID:  22681121     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Epistructural tension is the reversible work per unit area required to span the aqueous interface of a soluble protein structure. The parameter accounts for the free-energy cost of imperfect hydration, involving water molecules with a shortage of hydrogen-bonding partnerships relative to bulk levels. The binding hot spots along protein-protein interfaces are identified with residues that contribute significantly to the epistructural tension in the free subunits. Upon association, such residues either displace or become deprived of low-coordination vicinal water molecules.
Authors:
Ariel Fernández
Publication Detail:
Type:  Journal Article     Date:  2012-05-04
Journal Detail:
Title:  Physical review letters     Volume:  108     ISSN:  1079-7114     ISO Abbreviation:  Phys. Rev. Lett.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-06-11     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0401141     Medline TA:  Phys Rev Lett     Country:  United States    
Other Details:
Languages:  eng     Pagination:  188102     Citation Subset:  IM    
Affiliation:
Instituto Argentino de Matemática, CONICET (National Research Council), Saavedra 15, 1083 Buenos Aires, Argentina and Department of Computer Science, The University of Chicago, Chicago, Illinois 60637, USA and The Morgridge Institute for Research at the University of Wisconsin-Madison, Madison, Wisconsin 53715, USA.
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