A nanofiber assembly directed by the non-classical antiparallel β-structure from 4S-(OH) proline polypeptide

dc.contributor.author	Bansode, Nitin D.	en_US
dc.contributor.author	Sonar, Mahesh V.	en_US
dc.contributor.author	GANESH, KRISHNA N.	en_US
dc.date.accessioned	2019-04-26T09:12:30Z
dc.date.available	2019-04-26T09:12:30Z
dc.date.issued	2016-03	en_US
dc.identifier.citation	Chemical Communications, 52(27), 4884-4887.	en_US
dc.identifier.issn	1359-7345	en_US
dc.identifier.issn	1364-548X	en_US
dc.identifier.uri	http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/2496
dc.identifier.uri	https://doi.org/10.1039/C6CC00838K	en_US
dc.description.abstract	The antiparallel arrangement of two strands of the non-classical β-structure, formed exclusively via cis-4S-(OH) prolyl polypeptide as established by FRET, propagates into self-assembled nanofibers upon conjugation with C12/C14/C16 hydrocarbon chains.	en_US
dc.language.iso	en	en_US
dc.publisher	Royal Society of Chemistry	en_US
dc.subject	Nanofiber assembly	en_US
dc.subject	Non-classical antiparallel	en_US
dc.subject	Proline polypeptide	en_US
dc.subject	Conformation in protein unfolding	en_US
dc.subject	2016	en_US
dc.title	A nanofiber assembly directed by the non-classical antiparallel β-structure from 4S-(OH) proline polypeptide	en_US
dc.type	Article	en_US
dc.contributor.department	Dept. of Chemistry	en_US
dc.identifier.sourcetitle	Chemical Communications	en_US
dc.publication.originofpublisher	Foreign	en_US