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 language | English |
|---|---|
| Pages (from-to) | 1002-1011 |
| Number of pages | 10 |
| Journal | Biopolymers |
| Volume | 89 |
| Issue number | 11 |
| DOIs | |
| State | Published - Nov 2008 |
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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 journal › Article
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TY - JOUR
T1 - The rote of weakly polar and H-bonding interactions in the stabilization of the conformers of FGG, WGG, and YGG
T2 - An aqueous phase computational study
AU - Csontos, József
AU - Murphy, Richard F.
AU - Lovas, Sándor
PY - 2008/11
Y1 - 2008/11
N2 - 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.
AB - 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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U2 - 10.1002/bip.21049
DO - 10.1002/bip.21049
M3 - Article
VL - 89
SP - 1002
EP - 1011
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 11
ER -