Helix Forming Tendency of Valine Substituted Poly-Alanine: A Molecular Dynamics Investigation
In this study, classical molecular dynamics simulations have been carried out on the valine (guest) substituted poly alanine (host) using the host−guest peptide approach to understand the role of valine in the formation and stabilization of helix. Valine has been substituted in the host peptide star...
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Published in | The journal of physical chemistry. B Vol. 112; no. 30; pp. 9100 - 9104 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
31.07.2008
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Subjects | |
Online Access | Get full text |
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Summary: | In this study, classical molecular dynamics simulations have been carried out on the valine (guest) substituted poly alanine (host) using the host−guest peptide approach to understand the role of valine in the formation and stabilization of helix. Valine has been substituted in the host peptide starting from N terminal to C terminal. Various structural parameters have been obtained from the molecular dynamics simulation to understand the tolerance of helical motif to valine. Depending on the position of valine in the host peptide, it stabilizes (or destabilizes) the formation of the helical structure. The substitution of valine in the poly alanine at some positions has no effect on the helix formation (deformation). It is interesting to observe the coexistence of 310 and α-helix in the peptides due to the dynamical nature of the hydrogen bonding interaction and sterical interactions. |
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Bibliography: | istex:F56B1BAFC5DF7B4B1BB67E6374474C23AD9CE076 Additional figures and an additional table. This material is available free of charge via the Internet at http://pubs.acs.org. ark:/67375/TPS-M7F13Q19-3 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1520-6106 1520-5207 |
DOI: | 10.1021/jp7119813 |