Protein-water hydrogen bonds are stabilized by electrostatic polarization

Ya Gao, Man Guo, Ye Mei, John Zhang

Research output: Contribution to journalArticle

Abstract

We study the dynamical properties of the hydration water around apo-myoglobin in this work under traditional AMBER force field and the polarized protein-specific charges (PPC). Both SPC/E and TIP3P water models are utilized in order to reveal the model dependence. With polarization effect taken into consideration as in the PPC, the hydrogen bonds between the protein and the solvation water molecules are strengthened. Therefore the lifetime of the hydrogen bonds increases, and both the rotational and translational motions of the water molecules are hindered. We also notice that these results have apparent model dependence, when comparing the SPC/E and TIP3P water models.

Original languageEnglish (US)
Pages (from-to)595-604
Number of pages10
JournalMolecular Physics
Volume110
Issue number9-10
DOIs
StatePublished - May 10 2012

Fingerprint

Static Electricity
Hydrogen
Electrostatics
Hydrogen bonds
Polarization
electrostatics
hydrogen bonds
proteins
Water
polarization
water
Proteins
myoglobin
Molecules
translational motion
Myoglobin
Solvation
Hydration
field theory (physics)
solvation

Keywords

  • Einstein diffusion constant
  • electrostatic polarization
  • hydration water
  • residence
  • rotational diffusion

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Condensed Matter Physics
  • Biophysics
  • Molecular Biology

Cite this

Protein-water hydrogen bonds are stabilized by electrostatic polarization. / Gao, Ya; Guo, Man; Mei, Ye; Zhang, John.

In: Molecular Physics, Vol. 110, No. 9-10, 10.05.2012, p. 595-604.

Research output: Contribution to journalArticle

Gao, Ya ; Guo, Man ; Mei, Ye ; Zhang, John. / Protein-water hydrogen bonds are stabilized by electrostatic polarization. In: Molecular Physics. 2012 ; Vol. 110, No. 9-10. pp. 595-604.
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