Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/2501
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dc.contributor.authorMisra, Rajkumaren_US
dc.contributor.authorReja, Rahi M.en_US
dc.contributor.authorNarendra, Lagumaddepalli V.en_US
dc.contributor.authorGeorge, Gijoen_US
dc.contributor.authorRaghothama, Srinivasaraoen_US
dc.contributor.authorGOPI, HOSAHUDYA N.en_US
dc.date.accessioned2019-04-26T09:12:30Z
dc.date.available2019-04-26T09:12:30Z
dc.date.issued2016-06en_US
dc.identifier.citationChemical Communications, 52(61), 9597-9600.en_US
dc.identifier.issn1359-7345en_US
dc.identifier.issn1364-548Xen_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/2501-
dc.identifier.urihttps://doi.org/10.1039/C6CC04502Ben_US
dc.description.abstractWe are reporting the influence of foldamer structures on their self-assembled architectures. In a sharp contrast to the ordered α,γ-hybrid 12-helix obtained from 1 : 1 alternating Aib and γ-Phe, the α,γ-hybrid peptides constituted with α-Phe and 4,4-dimethyl γ-amino acid (Aic) displayed the extended sheet type of conformations in solution and spontaneously self-assembled into thermally and proteolytically stable capsules. In contrast, the conformationally ordered 12-helix self-assembled into a three-dimensional supramolecular polyhedron.en_US
dc.language.isoenen_US
dc.publisherRoyal Society of Chemistryen_US
dc.subjectExploring structural featuresen_US
dc.subjectFolded peptideen_US
dc.subjectArchitecturesen_US
dc.subjectConstruction of nanomaterialsen_US
dc.subjectArtificial buildingen_US
dc.subject2016en_US
dc.titleExploring structural features of folded peptide architectures in the construction of nanomaterialsen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleChemical Communicationsen_US
dc.publication.originofpublisherForeignen_US
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