Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/6785
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dc.contributor.authorSarmento, Ana Cristinapt
dc.contributor.authorOliveira, Cláudia S.pt
dc.contributor.authorPereira, Anabelapt
dc.contributor.authorEsteves, Valdemar I.pt
dc.contributor.authorMoir, Arthur J.G. Moirpt
dc.contributor.authorSaraiva, Jorgept
dc.contributor.authorPires, Euclidespt
dc.contributor.authorBarros, Marlenept
dc.date.accessioned2012-02-22T16:30:53Z-
dc.date.issued2009-
dc.identifier.issn1381-1177pt
dc.identifier.urihttp://hdl.handle.net/10773/6785-
dc.description.abstractIn the present study the relationship between conformational stability and enzymatic activity in the presence of organic solvents (OS) was investigated. We have found that cardosin A, the model protease investigated in this work, inactivates through a biphasic mechanism, which is incipient in aqueous buffer and becomes visible in the presence of hydrophilic OS. In fact, in OS this inactivation originates stable intermediaries thatwere detected in acetonitrile. This biphasic mechanism can be described in two phases: an initial one, where OS induce alterations that affect the active site cleft and global mobility, but with little interference on the global protein conformation, and, a second phase, where there is a global change in protein conformation with concomitant activity loss. It is shown that in the presence of hydrophilic OS there is a larger mobility of the enzyme, revealed by limited proteolysis, probably due to a weakening of hydrophobic interactions within the protein core.pt
dc.language.isoengpt
dc.publisherElsevierpt
dc.relationPOCI/QUI/60791/2004pt
dc.relationFCT - BPD-7183/2001pt
dc.relationFCT - BPD-26670/2006pt
dc.relationFCT - BPD/26685/2006pt
dc.rightsrestrictedAccesspor
dc.subjectAspartic proteinasespt
dc.subjectOrganic solventspt
dc.subjectFoldingpt
dc.subjectIntermediariespt
dc.titleUnfolding of cardosin A in organic solvents and detection of intermediariespt
dc.typearticlept
dc.peerreviewedyespt
ua.distributioninternationalpt
degois.publication.firstPage115pt
degois.publication.issue1-4
degois.publication.issue1-4pt
degois.publication.lastPage122pt
degois.publication.titleJournal of Molecular Catalysis B: Enzymaticpt
degois.publication.volume57pt
dc.date.embargo10000-01-01-
dc.identifier.doi10.1016/j.molcatb.2008.08.004*
Appears in Collections:DQ - Artigos
QOPNA - Artigos

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