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Huge disulfide-linkage's reductible potential variation induced by alpha-helix

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dc.contributor.authorDumont, Elise
dc.contributor.authorLoos, Pierre-Francois
dc.contributor.authorLaurent, Adele D
dc.contributor.authorAssfeld, Xavier
dc.date.accessioned2015-12-10T22:38:48Z
dc.date.issued2008
dc.date.updated2015-12-09T10:44:17Z
dc.description.abstractAn active site containing a Cys-X-X-Cys motif (CXXC), where X denotes any amino acid, is always found in the thiol-disulfide oxidoreductase superfamily. Because of its very high propensity for N-termini of α-helices, we examine the effect of this seconda
dc.identifier.issn1549-9618
dc.identifier.urihttp://hdl.handle.net/1885/56889
dc.publisherAmerican Chemical Society
dc.sourceJournal of Chemical Theory and Computation (JCTC)
dc.titleHuge disulfide-linkage's reductible potential variation induced by alpha-helix
dc.typeJournal article
local.bibliographicCitation.issue8
local.bibliographicCitation.lastpage1173
local.bibliographicCitation.startpage1171
local.contributor.affiliationDumont, Elise, Nancy-Universite
local.contributor.affiliationLoos, Pierre-Francois, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationLaurent, Adele D, Nancy-Universite
local.contributor.affiliationAssfeld, Xavier, Nancy-Universite
local.contributor.authoruidLoos, Pierre-Francois, u4622940
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030799 - Theoretical and Computational Chemistry not elsewhere classified
local.identifier.ariespublicationu4005981xPUB379
local.identifier.citationvolume4
local.identifier.doi10.1021/ct800161m
local.identifier.scopusID2-s2.0-55949106422
local.identifier.thomsonID000258400600001
local.type.statusPublished Version

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