Solvent Effects on the Secondary Structures of Proteins
Changmoon Park, Matt J. Carlson, William A. Goddard III
2000J. Phys. Chem. A, 104(11), 2498-250319cited
Abstract
We examined the effect of solvation on the conformational preferences (e.g., α-helix versus β-sheet) of tripeptides using ab initio quantum mechanics (Hartree−Fock 6-31G**) with solvation in the Poisson−Boltzmann continuum solvent approximation. We find that aqueous solvent preferentially stabilizes the α-helix conformation over β-sheet conformations by 3.5 kcal/mol for Ala, 2.4 kcal/mol for Gly, and 2.0 kcal/mol for Pro. We determined the torsional potential surfaces of the tripeptides, Gly-Ala-Gly, Gly-Gly-Gly, and Gly-Pro-Gly using both aqueous solvent and nonpolar solvent conditions. These results were used to determine force-field torsional parameters for the protein main chains.
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Cite this publication
Park, C., Carlson, M. J., & III, W. A. G. (2000). Solvent Effects on the Secondary Structures of Proteins. *J. Phys. Chem. A*, *104*(11), 2498-2503. https://doi.org/10.1021/jp9911189