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. https://resolver.caltech.edu/CaltechAUTHORS:20161129-131523601

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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.

Item Type:

Article

Related URLs:

URL	URL Type	Description
http://dx.doi.org/10.1021/jp9911189	DOI	Article
http://pubs.acs.org/doi/abs/10.1021/jp9911189	Publisher	Article
http://pubs.acs.org/doi/suppl/10.1021/jp9911189	Publisher	Supporting Information

ORCID:

Author	ORCID
Goddard, William A., III	0000-0003-0097-5716

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.

Funders:

Funding Agency	Grant Number
Department of Energy (DOE)	UNSPECIFIED
NSF	ASC 92-17368
NSF	CHE 95-22179
BP Chemical	UNSPECIFIED
Chevron Corporation	UNSPECIFIED
NASA	UNSPECIFIED
Caltech Beckman Institute	UNSPECIFIED
Army Research Office (ARO)	UNSPECIFIED
Seiko-Epson	UNSPECIFIED
Exxon	UNSPECIFIED
Saudi Aramco	UNSPECIFIED
Owens-Corning	UNSPECIFIED
Asahi Chemical	UNSPECIFIED
Office of Naval Research (ONR)	UNSPECIFIED
Avery–Dennison Corp.	UNSPECIFIED

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Record Number:

CaltechAUTHORS:20161129-131523601

Persistent URL:

https://resolver.caltech.edu/CaltechAUTHORS:20161129-131523601

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

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ID Code:

72409

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CaltechAUTHORS

Deposited By:

George Porter

Deposited On:

29 Nov 2016 21:40

Last Modified:

03 Oct 2019 16:17

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