Effect of the ordered interfacial water layer in protein complex formation: A nonlocal electrostatic approach

Using a nonlocal electrostatic approach that incorporates the short-range structure of the contacting media, we evaluated the electrostatic contribution to the energy of the complex formation of two model proteins. In this study, we have demonstrated that the existence of an ordered interfacial wate...

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Bibliographic Details
Published inPhysical review. E, Statistical, nonlinear, and soft matter physics Vol. 82; no. 2 Pt 1; p. 021915
Main Authors Rubinstein, A, Sabirianov, R F, Mei, W N, Namavar, F, Khoynezhad, A
Format Journal Article
LanguageEnglish
Published United States 01.08.2010
Subjects
Computer Simulation
Energy Transfer
Models, Chemical
Models, Molecular
Multiprotein Complexes - chemistry
Multiprotein Complexes - ultrastructure
Protein Conformation
Proteins - chemistry
Proteins - ultrastructure
Static Electricity
Surface Properties
Water - chemistry
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Summary:Using a nonlocal electrostatic approach that incorporates the short-range structure of the contacting media, we evaluated the electrostatic contribution to the energy of the complex formation of two model proteins. In this study, we have demonstrated that the existence of an ordered interfacial water layer at the protein-solvent interface reduces the charging energy of the proteins in the aqueous solvent, and consequently increases the electrostatic contribution to the protein binding (change in free energy upon the complex formation of two proteins). This is in contrast with the finding of the continuum electrostatic model, which suggests that electrostatic interactions are not strong enough to compensate for the unfavorable desolvation effects.
ISSN:1550-2376
DOI:10.1103/PhysRevE.82.021915