Document Detail


Protein aggregation reactions: surface free energy model.
MedLine Citation:
PMID:  7967625     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The energetics of protein reactions can be evaluated in terms of the surface free-energy model, an approach that estimates changes in the surface free energy of proteins from changes in the area and the charge density of the protein-water interface. This approach has given insight into the reactions of proteins in solution as well as in membranes (receptors and voltage-gated channels). The model highlights the importance of pH and thermal changes in aggregation reactions. It also enables a correct interpretation of the Hill equation describing co-operative reactions, since the Hill coefficient is related to a Gibbs surface excess that varies with the degree of reaction.
Authors:
M Blank
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of theoretical biology     Volume:  169     ISSN:  0022-5193     ISO Abbreviation:  J. Theor. Biol.     Publication Date:  1994 Aug 
Date Detail:
Created Date:  1994-12-16     Completed Date:  1994-12-16     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0376342     Medline TA:  J Theor Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  323-6     Citation Subset:  IM    
Affiliation:
Department of Physiology and Cellular Biophysics, Columbia University, College of Physicians & Surgeons, New York, NY 10032.
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MeSH Terms
Descriptor/Qualifier:
Chemistry, Physical
Hydrogen-Ion Concentration
Mathematics
Models, Chemical*
Physicochemical Phenomena
Proteins / chemistry*
Water / chemistry
Chemical
Reg. No./Substance:
0/Proteins; 7732-18-5/Water

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


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