Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/30953
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dc.contributor.authorMaestro García-Donas, Beatriz-
dc.contributor.authorSanz, Jesús M.-
dc.date.accessioned2024-02-02T09:31:40Z-
dc.date.available2024-02-02T09:31:40Z-
dc.date.created2006-
dc.identifier.citationFEBS Letters . 2007 Feb 6;581(3):375-81es_ES
dc.identifier.issn1873-3468-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://hdl.handle.net/11000/30953-
dc.description.abstractWe have investigated the stability of the choline-binding module C-LytA against sodium dodecyl sulphate (SDS)-induced unfolding at pH 7.0 and 20 C. A major intermediate with an unfolded N-terminal region accumulates at around 0.75 mM SDS, whereas 2.0 mM SDS was sufficient for a complete unfolding. This might be the first report of a protein being extensively unfolded by submicellar concentrations of SDS, occurring through formation of detergent clusters on the protein surface. All transitions were reversible upon SDS complexation with b-cyclodextrin, allowing the calculation of thermodynamic parameters. A model for the unfolding of C-LytA by SDS is presented and compared to a previous denaturation scheme by guanidine hydrochloride.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent7es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCholine-binding modulees_ES
dc.subjectSDS denaturationes_ES
dc.subjectProtein stabilityes_ES
dc.subjectRepeat proteinses_ES
dc.subjectAffinity tages_ES
dc.titleExtensive unfolding of the C-LytA choline-binding module by submicellar concentrations of sodium dodecyl sulphatees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.contributor.instituteInstitutos de la UMH::Instituto de Bioingenieríaes_ES
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