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A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin

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dc.contributor.authorTreweek, Teresa
dc.contributor.authorRekas, Agata
dc.contributor.authorWalker, Mark J.
dc.contributor.authorCarver, John
dc.date.accessioned2015-12-10T23:08:54Z
dc.date.issued2010
dc.date.updated2016-02-24T10:45:38Z
dc.description.abstractThe principal lens proteins αA- and αB-crystallin are members of the small heat-shock protein (sHsp) family of molecular chaperone proteins. Via their chaperone action, αA- and αB-crystallin play an important role in maintaining lens transparency by p
dc.identifier.issn0014-4835
dc.identifier.urihttp://hdl.handle.net/1885/63298
dc.publisherAcademic Press
dc.sourceExperimental Eye Research
dc.subjectKeywords: alpha crystallin; alpha lactalbumin; beta crystallin; chaperone; article; carboxy terminal sequence; heteronuclear single quantum coherence; lens; mutant; nitrogen nuclear magnetic resonance; nuclear magnetic resonance spectroscopy; nuclear Overhauser eff C-terminal extension; Molecular chaperone; NMR Spectroscopy; Site directed mutagenesis; Small heat-shock protein
dc.titleA quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin
dc.typeJournal article
local.bibliographicCitation.issue5
local.bibliographicCitation.lastpage699
local.bibliographicCitation.startpage691
local.contributor.affiliationTreweek, Teresa, University of Wollongong
local.contributor.affiliationRekas, Agata, ANSTO
local.contributor.affiliationWalker, Mark J., University of Queensland
local.contributor.affiliationCarver, John, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidCarver, John, u1571001
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationU4217927xPUB790
local.identifier.citationvolume91
local.identifier.doi10.1016/j.exer.2010.08.015
local.identifier.scopusID2-s2.0-78049506985
local.identifier.thomsonID000283826300017
local.type.statusPublished Version

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