Show simple item record

dc.contributor.authorTan, Yi Leien
dc.contributor.authorMitchell, Jamesen
dc.contributor.authorKlein-Seetharaman, Judithen
dc.contributor.authorNietlispach, Danielen
dc.date.accessioned2018-11-08T00:30:46Z
dc.date.available2018-11-08T00:30:46Z
dc.date.issued2018-10en
dc.identifier.issn0022-2836
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/284746
dc.description.abstractOur understanding on the folding of membrane proteins lags behind that of soluble proteins due to challenges posed by the exposure of hydrophobic regions during in vitro chemical denaturation and refolding experiments. While different folding models are accepted for soluble proteins, only the two-stage model and the long-range interactions model have been proposed so far for helical membrane proteins. To address our knowledge gap on how different membrane proteins traverse their folding pathways, we have systematically investigated the structural features of SDS-denatured states and the kinetics for reversible unfolding of sensory rhodopsin II (pSRII), a retinal-binding photophobic receptor from Natronomonas pharaonis. pSRII is difficult to denature, and only SDS can dislodge the retinal chromophore without rapid aggregation. Even in 30% SDS (0.998 ΧSDS) pSRII retains the equivalent of six out of seven transmembrane helices, while the retinal binding pocket is disrupted, with transmembrane residues becoming more solvent-exposed. Folding of pSRII from an SDS-denatured state harbouring a covalently-bound retinal chromophore shows deviations from an apparent two-state behaviour. SDS-denaturation to form the sensory opsin apo-protein is reversible. We report pSRII as a new model protein which is suitable for membrane protein folding studies, and has a unique folding mechanism that differs from those of bacteriorhodopsin and bovine rhodopsin.
dc.description.sponsorshipBBSRC
dc.format.mediumPrint-Electronicen
dc.languageengen
dc.publisherElsevier
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectAnimalsen
dc.subjectCattleen
dc.subjectBacteriorhodopsinsen
dc.subjectSensory Rhodopsinsen
dc.subjectSolventsen
dc.subjectProtein Conformationen
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Bindingen
dc.subjectProtein Denaturationen
dc.subjectProtein Foldingen
dc.subjectKineticsen
dc.subjectProtein Unfoldingen
dc.subjectProtein Refoldingen
dc.titleCharacterization of Denatured States and Reversible Unfolding of Sensory Rhodopsin II.en
dc.typeArticle
prism.endingPage4086
prism.issueIdentifier21en
prism.publicationDate2018en
prism.publicationNameJournal of molecular biologyen
prism.startingPage4068
prism.volume430en
dc.identifier.doi10.17863/CAM.32118
dcterms.dateAccepted2018-07-23en
rioxxterms.versionofrecord10.1016/j.jmb.2018.07.031en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2018-10en
dc.contributor.orcidTan, Yi Lei [0000-0002-4013-3225]
dc.contributor.orcidNietlispach, Daniel [0000-0003-4364-9291]
dc.identifier.eissn1089-8638
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idBBSRC (BB/K01983X/1)
pubs.funder-project-idBBSRC (BB/G011915/1)
rioxxterms.freetoread.startdate2019-08-09


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-NoDerivatives 4.0 International
Except where otherwise noted, this item's licence is described as Attribution-NonCommercial-NoDerivatives 4.0 International