ArticleJournal of molecular modeling2008
Structural and dynamical studies of all-trans and all-cis cyclo[(1R,3S)-gamma-Acc-Gly]3 peptides.
Article in Journal of molecular modeling, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Cyclo-hexa-peptides at the water/cyclohexane interface: a molecular dynamics simulation.Journal of molecular modeling · 2013Article
- Structural analysis and the effect of cyclo(His-Pro) dipeptide on neurotoxins--a dynamics and density functional theory study.Journal of molecular modeling · 2010Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The quantum chemical and molecular dynamics studies have been performed to infer the structural changes of all-trans and all-cis forms of cyclo[(1R,3S)-3-aminocyclohexanecarboxylicacid(gamma-Acc)-alpha-Glycine(Gly)](3) hexapeptide. The backbone conformations of the above peptide have been analyzed using the valence and peptide deformation angles applying B3LYP/6-311G** level of theory. The conformational preference of the backbone of all-trans and all-cis cyclo[(1R,3S)-gamma-Acc-Gly](3) hexapeptides is found to depend on the puckering of cyclohexane rings. The non-uniform distribution of water inside the cavity is observed, where sometimes water molecules formed a chain like conformation through hydrogen bond networks while traversing the pore of all-cis cyclo[(1R,3S)-gamma-Acc-Gly](3) peptide. Larger relaxation times of the order of a hundred to two hundred pico seconds for active site...water hydrogen bond interactions were noticed. The hydrophobic nature of the cavity of all-trans cyclo[(1R,3S)-gamma-Acc-Gly](3) due to the presence of cyclohexane moiety has been analyzed. Further this investigation emphasized on the non-transport of molecules through the pore of all-trans cyclo[(1R,3S)-gamma-Acc-Gly](3) peptide due to the obstruction produced by cyclohexane groups.
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Registered trials
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