| Direct allowance for the effects of thermodynamic nonideality in the quantitative characterization of protein self-association by osmometry. | |
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MedLine Citation:
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PMID: 19782460 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Peter R Wills; Donald J Winzor |
Publication Detail:
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Type: Journal Article Date: 2009-09-11 |
Journal Detail:
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Title: Biophysical chemistry Volume: 145 ISSN: 1873-4200 ISO Abbreviation: Biophys. Chem. Publication Date: 2009 Dec |
Date Detail:
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Created Date: 2009-10-27 Completed Date: 2010-01-22 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0403171 Medline TA: Biophys Chem Country: Netherlands |
Other Details:
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Languages: eng Pagination: 64-71 Citation Subset: IM |
Affiliation:
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School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Membrane
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metabolism Chymotrypsin / chemistry, metabolism Hemoglobins / chemistry, metabolism Humans Hydrogen-Ion Concentration Models, Molecular Osmotic Pressure Protease Inhibitors / chemistry, metabolism Protein Multimerization* Protein Structure, Quaternary Soybean Proteins / chemistry, metabolism Soybeans / enzymology Static Electricity Thermodynamics* |
| Chemical | |
Reg. No./Substance:
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0/Hemoglobins; 0/Protease Inhibitors; 0/Soybean Proteins; EC 3.4.21.1/Chymotrypsin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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