Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/39237
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dc.contributor.authorSánchez-Hidalgo, Marina-
dc.contributor.authorFernández-Escamilla, Ana Mª-
dc.contributor.authorMartínez-Bueno, Manuel-
dc.contributor.authorValdivia, Eva-
dc.contributor.authorSerrano, Luis-
dc.contributor.authorMaqueda, Mercedes-
dc.contributor.otherDepartamentos de la UMH::Bioquímica y Biología Moleculares_ES
dc.date.accessioned2026-02-12T13:31:02Z-
dc.date.available2026-02-12T13:31:02Z-
dc.date.created2010-06-
dc.identifier.citationProtein & Peptide Letters, Vol. 17, Nº 6 (2010)es_ES
dc.identifier.issn1875-5305-
dc.identifier.issn0929-8665-
dc.identifier.urihttps://hdl.handle.net/11000/39237-
dc.description.abstractFour AS-48 mutants (Trp24Ala, Gly13Lys, Leu40Lys and Ala53Ser) were obtained by site-directed mutagenesis. The minimal inhibitory concentration of each peptide showed that only residue Trp24 was unquestionably involved in the biological activity. Guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation process, suggesting a molten-globule-like conformation after the first transition.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent7es_ES
dc.language.isoenges_ES
dc.publisherBentham Science Publisherses_ES
dc.rightsinfo:eu-repo/semantics/closedAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCircular antimicrobial peptideses_ES
dc.subjectSite-directed mutagenesises_ES
dc.subjectLactic-acid bacteriaes_ES
dc.subjectEnterococcies_ES
dc.titleConformational Stability and Activity of Circular Enterocin AS-48 Derivativeses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttps://doi.org/10.2174/092986610791190390es_ES
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Artículos - Bioquímica y Biología Molecular


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