Document Detail

Direct allowance for the effects of thermodynamic nonideality in the quantitative characterization of protein self-association by osmometry.
MedLine Citation:
PMID:  19782460     Owner:  NLM     Status:  MEDLINE    
A procedure is described for the direct analysis of osmotic pressure data for reversibly dimerizing proteins that makes allowance for effects of thermodynamic nonideality on the statistical-mechanical basis of the potential-of-mean-force between molecules. Detailed consideration is also given to calculation of the magnitudes of the required virial coefficients. After illustration of the approach with analysis of simulated osmotic pressure data, the method is used to obtain dimerization constants from published osmotic pressure data for soybean proteinase inhibitor, hemoglobin and alpha-chymotrypsin.
Peter R Wills; Donald J Winzor
Publication Detail:
Type:  Journal Article     Date:  2009-09-11
Journal Detail:
Title:  Biophysical chemistry     Volume:  145     ISSN:  1873-4200     ISO Abbreviation:  Biophys. Chem.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-10-27     Completed Date:  2010-01-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0403171     Medline TA:  Biophys Chem     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  64-71     Citation Subset:  IM    
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia.
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MeSH Terms
Cell Membrane / metabolism
Chymotrypsin / chemistry,  metabolism
Hemoglobins / chemistry,  metabolism
Hydrogen-Ion Concentration
Models, Molecular
Osmotic Pressure
Protease Inhibitors / chemistry,  metabolism
Protein Multimerization*
Protein Structure, Quaternary
Soybean Proteins / chemistry,  metabolism
Soybeans / enzymology
Static Electricity
Reg. No./Substance:
0/Hemoglobins; 0/Protease Inhibitors; 0/Soybean Proteins; EC

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