Chiral effects on helicity studied via the energy landscape of short (d, l)-alanine peptides

Sridhar Neelamraju; Mark T. Oakley; Roy L. Johnston

doi:10.1063/1.4933428

Chiral effects on helicity studied via the energy landscape of short (d, l)-alanine peptides

Sridhar Neelamraju^*, Mark T. Oakley, Roy L. Johnston

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

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Abstract

The homochirality of natural amino acids facilitates the formation of regular secondary structures such as α-helices and β-sheets. Here, we study the relationship between chirality and backbone structure for the example of hexa-alanine. The most stable stereoisomers are identified through global optimisation. Further, the energy landscape, a database of connected low-energy local minima and transition points, is constructed for various neutral and zwitterionic stereoisomers of hexa-alanine. Three order parameters for partial helicity are applied and metric disconnectivity graphs are presented with partial helicity as a metric. We also apply the Zimm-Bragg model to derive average partial helicities for Ace-(l-Ala)₆-NHMe, Ace-(d-Ala-l-Ala)₃-NHMe, and Ace-(l-Ala)₃-(d-Ala)₃-NHMe from the database of local minima and compare with previous studies.

Original language	English
Article number	165103
Journal	Journal of Chemical Physics
Volume	143
Issue number	16
DOIs	https://doi.org/10.1063/1.4933428
Publication status	Published - 2015

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1063/1.4933428

Neelamraju_et_al_Chiral_effects_helicity_Journal_Chemical_Physics_2015
Copyright (2015) American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics. The following article appeared in Neelamraju, Sridhar, Mark T. Oakley, and Roy L. Johnston. "Chiral effects on helicity studied via the energy landscape of short (d, l)-alanine peptides." The Journal of Chemical Physics 143.16 (2015): 165103. and may be found at http://dx.doi.org/10.1063/1.4933428 Checked November 2015
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abstract = "The homochirality of natural amino acids facilitates the formation of regular secondary structures such as α-helices and β-sheets. Here, we study the relationship between chirality and backbone structure for the example of hexa-alanine. The most stable stereoisomers are identified through global optimisation. Further, the energy landscape, a database of connected low-energy local minima and transition points, is constructed for various neutral and zwitterionic stereoisomers of hexa-alanine. Three order parameters for partial helicity are applied and metric disconnectivity graphs are presented with partial helicity as a metric. We also apply the Zimm-Bragg model to derive average partial helicities for Ace-(l-Ala)6-NHMe, Ace-(d-Ala-l-Ala)3-NHMe, and Ace-(l-Ala)3-(d-Ala)3-NHMe from the database of local minima and compare with previous studies.",

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Chiral effects on helicity studied via the energy landscape of short (d, l)-alanine peptides

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