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dc.contributor.authorG, Praveena-
dc.contributor.authorP, Kolandaivel-
dc.date.accessioned2020-09-24T05:32:04Z-
dc.date.available2020-09-24T05:32:04Z-
dc.date.issued2008-12-01-
dc.identifier.urihttps://link.springer.com/article/10.1007/s00894-008-0357-1-
dc.identifier.urihttp://localhost:8080/xmlui/handle/123456789/1651-
dc.description.abstractThe 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(γ-Acc)-α- 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)-γ-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)-γ-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)-γ-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)-γ-Acc-Gly]3 peptide due to the obstruction produced by cyclohexane groups.en_US
dc.language.isoenen_US
dc.publisherSpringer-Verlagen_US
dc.subjectDensity functional theoryen_US
dc.subjectHybrid α–γ cyclic peptideen_US
dc.subjectMetal ionsen_US
dc.subjectMolecular electrostatic potentialen_US
dc.subjectBinding energyen_US
dc.titleSTRUCTURAL AND DYNAMICAL STUDIES OF ALL-TRANS AND ALL-CIS CYCLO [(1R, 3S)-Γ-ACC-GLY] 3 PEPTIDESen_US
dc.typeArticleen_US
Appears in Collections:International Journals

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