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

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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
Issue number11
Publication statusPublished - Nov 2008


All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Biomaterials
  • Organic Chemistry

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