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

A. Rubinstein, R. F. Sabirianov, W. N. Mei, F. Namavar, A. Khoynezhad

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Article number021915
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Volume82
Issue number2
DOIs
StatePublished - Aug 18 2010

Fingerprint

Electrostatics
electrostatics
proteins
Protein
Water
water
Energy
charging
Free Energy
Continuum
free energy
continuums
energy
Interaction
Model
Range of data
interactions

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics

Cite this

Effect of the ordered interfacial water layer in protein complex formation : A nonlocal electrostatic approach. / Rubinstein, A.; Sabirianov, R. F.; Mei, W. N.; Namavar, F.; Khoynezhad, A.

In: Physical Review E - Statistical, Nonlinear, and Soft Matter Physics, Vol. 82, No. 2, 021915, 18.08.2010.

Research output: Contribution to journalArticle

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