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Solvent Effects on the Secondary Structures of Proteins

Park, Changmoon and Carlson, Matt J. and Goddard, William A., III (2000) Solvent Effects on the Secondary Structures of Proteins. Journal of Physical Chemistry A, 104 (11). pp. 2498-2503. ISSN 1089-5639. doi:10.1021/jp9911189.

[img] PDF (QM energies and solvation energies for all 39 conformations of all cases listed in Table 2. Tables S-1, S-2, and S-3 are for G-A-G, G-G-G, and G-P-C, respectively, and Table S-4 shows the special points for all cases) - Supplemental Material
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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.

Item Type:Article
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URLURL TypeDescription Information
Goddard, William A., III0000-0003-0097-5716
Additional Information:© 2000 American Chemical Society. Received: April 1, 1999; In Final Form: August 27, 1999. Publication Date (Web): November 6, 1999. This research was initiated under a grant from the Biological Chemical Technologies Research (BCTR) program of the Department of Energy and completed with funding from NSF (ASC 92-17368 and CHE 95-22179). The facilities of the MSC are also supported by grants from, BP Chemical, Chevron Corp., NASA, Beckman Institute, Army Research Office, Seiko-Epson, Exxon, Saudi Aramco, Owens-Corning, Asahi Chemical, ONR, and Avery-Dennison Corp. Some of these calculations were carried out at the NSF Supercomputer Centers in San Diego and Illinois, and on the JPL Cray.
Funding AgencyGrant Number
Department of Energy (DOE)UNSPECIFIED
NSFASC 92-17368
NSFCHE 95-22179
Chevron CorporationUNSPECIFIED
Caltech Beckman InstituteUNSPECIFIED
Army Research Office (ARO)UNSPECIFIED
Office of Naval Research (ONR)UNSPECIFIED
Avery–Dennison Corp.UNSPECIFIED
Issue or Number:11
Record Number:CaltechAUTHORS:20161129-131523601
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Official Citation:Solvent Effects on the Secondary Structures of Proteins Changmoon Park, Matt J. Carlson, and William A. Goddard, III The Journal of Physical Chemistry A 2000 104 (11), 2498-2503 DOI: 10.1021/jp9911189
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:72409
Deposited By: George Porter
Deposited On:29 Nov 2016 21:40
Last Modified:11 Nov 2021 05:00

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