Analysis of thermodynamic non-ideality in terms of protein solvation

Winzor, D. J., Carrington, L. E. and Harding, S. E. (2001) Analysis of thermodynamic non-ideality in terms of protein solvation. Biophysical Chemistry, 93 2-3: 231-240. doi:10.1016/S0301-4622(01)00223-X

Author Winzor, D. J.
Carrington, L. E.
Harding, S. E.
Title Analysis of thermodynamic non-ideality in terms of protein solvation
Journal name Biophysical Chemistry   Check publisher's open access policy
ISSN 0301-4622
Publication date 2001
Sub-type Article (original research)
DOI 10.1016/S0301-4622(01)00223-X
Volume 93
Issue 2-3
Start page 231
End page 240
Total pages 10
Place of publication Netherlands
Publisher Elsevier
Collection year 2001
Language eng
Subject C1
270100 Biochemistry and Cell Biology
780105 Biological sciences
Abstract The effects of thermodynamic non-ideality on the forms of sedimentation equilibrium distributions for several isoelectric proteins have been analysed on the statistical-mechanical basis of excluded volume to obtain an estimate of the extent of protein solvation. Values of the effective solvation. parameter delta are reported for ellipsoidal as well as spherical models of the proteins, taken to be rigid, impenetrable macromolecular structures. The dependence of the effective solvated radius upon protein molecular mass exhibits reasonable agreement with the relationship calculated for a model in which the unsolvated protein molecule is surrounded by a 0.52-nm solvation shell. Although the observation that this shell thickness corresponds to a double layer of water molecules may be of questionable relevance to mechanistic interpretation of protein hydration, it augurs well for the assignment of magnitudes to the second virial coefficients of putative complexes in the quantitative characterization of protein-protein interactions under conditions where effects of thermodynamic non-ideality cannot justifiably be neglected. (C) 2001 Elsevier Science B.V. All rights reserved.
Keyword Biochemistry & Molecular Biology
Chemistry, Physical
Protein Solvation
Sedimentation Equilibrium
Thermodynamic Non-ideality
Virial Coefficients
Sedimentation Equilibrium Experiments
Macromolecular Solutions
Muscle Aldolase
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 23 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 14 Aug 2007, 15:18:25 EST