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

10.1371/journal.pone.0134823

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Main Authors:	GARVITA GUPTA, Lim L., Song J.
Other Authors:	DUKE-NUS MEDICAL SCHOOL
Format:	Article
Published:	Public Library of Science 2018
Online Access:	http://scholarbank.nus.edu.sg/handle/10635/142907
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1429072023-10-26T07:28:29Z 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 GARVITA GUPTA Lim L. Song J. DUKE-NUS MEDICAL SCHOOL BIOLOGY (NU) 10.1371/journal.pone.0134823 PLoS ONE 10 8 e0134823 2018-06-06T08:52:10Z 2018-06-06T08:52:10Z 2015 Article 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 19326203 http://scholarbank.nus.edu.sg/handle/10635/142907 000359352600026 Public Library of Science Scopus
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
description	10.1371/journal.pone.0134823
author2	DUKE-NUS MEDICAL SCHOOL
author_facet	DUKE-NUS MEDICAL SCHOOL GARVITA GUPTA Lim L. Song J.
format	Article
author	GARVITA GUPTA Lim L. Song J.
spellingShingle	GARVITA GUPTA Lim L. Song J. 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
author_sort	GARVITA GUPTA
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
title_short	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
title_full	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
title_fullStr	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
title_full_unstemmed	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
title_sort	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
publisher	Public Library of Science
publishDate	2018
url	http://scholarbank.nus.edu.sg/handle/10635/142907
_version_	1781791305908617216

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

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