The rote of weakly polar and H-bonding interactions in the stabilization of the conformers of FGG, WGG, and YGG: An aqueous phase computational study

József Csontos, Richard F. Murphy, Sándor Lovas

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The energetics of intramolecular interactions on the conformational potential energy surface of the terminally protected N-Ac-Phe-Gly-Gly-NHMe (FGG), N-Ac-Trp-Gly-Gly-NHMe (WGG), and N-Ac-Tyr-Gly-Gly-NHMe (YGG) tripeptides was investigated. To identify the representative conformations, simulated annealing molecular dynamics (MD) and density functional theory (DFT) methods were used. The interaction energies were calculated at the BHandHLYP/aug-cc-pVTZ level of theory. In the global minima, 10%, 31%, and 10% of the stabilization energy come from weakly polar interactions, respectively, in FGG, WGG, and YGG. In the prominent cases 46%, 62%, and 46% of the stabilization energy is from the weakly polar interactions, respectively, in FGG, WGG, and YGG. On average, weakly polar interactions account for 15%, 34%, and 9% of the stabilization energies of the FGG, WGG, and YGG conformers, respectively. Thus, weakly polar interactions can make an important energetic contribution to protein structure and function.

Original languageEnglish
Pages (from-to)1002-1011
Number of pages10
JournalBiopolymers
Volume89
Issue number11
DOIs
StatePublished - Nov 2008

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Stabilization
tyrosyl-glycyl-glycine
Potential energy surfaces
Molecular Dynamics Simulation
Simulated annealing
Density functional theory
Conformations
Molecular dynamics
Proteins
N-acetylglycylglycine

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Biomaterials
  • Organic Chemistry

Cite this

The rote of weakly polar and H-bonding interactions in the stabilization of the conformers of FGG, WGG, and YGG : An aqueous phase computational study. / Csontos, József; Murphy, Richard F.; Lovas, Sándor.

In: Biopolymers, Vol. 89, No. 11, 11.2008, p. 1002-1011.

Research output: Contribution to journalArticle

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abstract = "The energetics of intramolecular interactions on the conformational potential energy surface of the terminally protected N-Ac-Phe-Gly-Gly-NHMe (FGG), N-Ac-Trp-Gly-Gly-NHMe (WGG), and N-Ac-Tyr-Gly-Gly-NHMe (YGG) tripeptides was investigated. To identify the representative conformations, simulated annealing molecular dynamics (MD) and density functional theory (DFT) methods were used. The interaction energies were calculated at the BHandHLYP/aug-cc-pVTZ level of theory. In the global minima, 10{\%}, 31{\%}, and 10{\%} of the stabilization energy come from weakly polar interactions, respectively, in FGG, WGG, and YGG. In the prominent cases 46{\%}, 62{\%}, and 46{\%} of the stabilization energy is from the weakly polar interactions, respectively, in FGG, WGG, and YGG. On average, weakly polar interactions account for 15{\%}, 34{\%}, and 9{\%} of the stabilization energies of the FGG, WGG, and YGG conformers, respectively. Thus, weakly polar interactions can make an important energetic contribution to protein structure and function.",
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