Quantifying the stabilizing energy of the intraprotein hydrogen bond due to local mutation

Chang G. Ji, John Zhang

Research output: Contribution to journalArticle

Abstract

MD simulation of the WW domain of PIN based on a dynamically adjusted polarized protein-specific force field from quantum fragment calculations is carried out in both wild and VAL22ALA mutant states. The result shows that the geometry of the Arg14-TYR23 hydrogen bond is conserved upon mutation of VAL22 to ALA. However, the electrostatic energy of this hydrogen bond in the mutant is found to be 0.6 kcal/mol weaker than in the wild state, in close agreement with the experimentally measured upper limit of 1.2 kcal/mol. Analysis shows that the weakened energy of this hydrogen bond in the mutant is due to its dynamically changed polarization resulting from an altered local electrostatic environment near the hydrogen bond which becomes more exposed to the solvent than in the wild.

Original languageEnglish (US)
Pages (from-to)12230-12233
Number of pages4
JournalJournal of Physical Chemistry B
Volume115
Issue number42
DOIs
StatePublished - Oct 27 2011

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mutations
Hydrogen bonds
hydrogen bonds
Electrostatics
electrostatics
energy
field theory (physics)
fragments
Polarization
proteins
Proteins
Geometry
polarization
geometry
simulation

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Quantifying the stabilizing energy of the intraprotein hydrogen bond due to local mutation. / Ji, Chang G.; Zhang, John.

In: Journal of Physical Chemistry B, Vol. 115, No. 42, 27.10.2011, p. 12230-12233.

Research output: Contribution to journalArticle

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