NMR and MD studies reveal that the isolated dengue NS3 protease is an intrinsically disordered chymotrypsin fold which absolutely requests NS2B for correct folding and functional dynamics

Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0134823

DC Field	Value
dc.title	NMR and MD studies reveal that the isolated dengue NS3 protease is an intrinsically disordered chymotrypsin fold which absolutely requests NS2B for correct folding and functional dynamics
dc.contributor.author	GARVITA GUPTA
dc.contributor.author	Lim L.
dc.contributor.author	Song J.
dc.date.accessioned	2018-06-06T08:52:10Z
dc.date.available	2018-06-06T08:52:10Z
dc.date.issued	2015
dc.identifier.citation	GARVITA GUPTA, Lim L., Song J. (2015). NMR and MD studies reveal that the isolated dengue NS3 protease is an intrinsically disordered chymotrypsin fold which absolutely requests NS2B for correct folding and functional dynamics. PLoS ONE 10 (8) : e0134823. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0134823
dc.identifier.issn	19326203
dc.identifier.uri	http://scholarbank.nus.edu.sg/handle/10635/142907
dc.publisher	Public Library of Science
dc.source	Scopus
dc.type	Article
dc.contributor.department	DUKE-NUS MEDICAL SCHOOL
dc.contributor.department	BIOLOGY (NU)
dc.description.doi	10.1371/journal.pone.0134823
dc.description.sourcetitle	PLoS ONE
dc.description.volume	10
dc.description.issue	8
dc.description.page	e0134823
dc.identifier.isiut	000359352600026
Appears in Collections:	Staff Publications Elements

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