Allowance for thermodynamic nonideality in the characterization of protein interactions by spectral techniques

Wills, Peter R. and Winzor, Donald J. (2011) Allowance for thermodynamic nonideality in the characterization of protein interactions by spectral techniques. Biophysical Chemistry, 158 1: 21-25. doi:10.1016/j.bpc.2011.04.011


Author Wills, Peter R.
Winzor, Donald J.
Title Allowance for thermodynamic nonideality in the characterization of protein interactions by spectral techniques
Journal name Biophysical Chemistry   Check publisher's open access policy
ISSN 0301-4622
1873-4200
Publication date 2011-09
Sub-type Article (original research)
DOI 10.1016/j.bpc.2011.04.011
Volume 158
Issue 1
Start page 21
End page 25
Total pages 5
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Collection year 2012
Language eng
Formatted abstract
Theory is developed for the characterization of protein interactions by spectral techniques, where the constraints of constant temperature and pressure demand that thermodynamic activity be defined on the molal concentration scale. The customary practice of defining the equilibrium constant (K) on a molar basis is accommodated by developing expressions to convert those experimental values (Kmolar) to their thermodynamically more rigorous counterparts (Kmolal). Such procedures are illustrated by reanalysis of published results for the effects of molecular crowding agents on the isomerisation of α-chymotrypsin and reversible complex formation between catalase and superoxide dismutase. Although those reanalyses have led to only minor refinements of the quantitative interpretation, it is clearly preferable to adopt thermodynamic rigor throughout future spectral studies by employing the molal concentration scale from the outset.
Keyword Difference spectroscopy
Fluorescence quenching
Molecular crowding
Protein-protein interactions
Thermodynamic nonideality
Excluded-volume
Conformation
Erythrocuprein
Chymotrypsin
Association
Temperature
Equilibria
Glycols
Ph
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
 
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