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Unfolding kinetics of beta-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study

2007-11Journal article Open access
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dc.contributor.authorViseu, Maria Isabel
dc.contributor.authorEP, Melo
dc.contributor.authorCarvalho, Teresa Isabel
dc.contributor.authorCorreia, Raquel F.
dc.contributor.authorCosta, Silvia M. B.
dc.date.accessioned2018-12-07T14:58:01Z
dc.date.available2018-12-07T14:58:01Z
dc.date.issued2007-11
dc.description.abstractThe beta ->alpha transition of beta-lactoglobulin, a globular protein abundant in the milk of several mammals, is investigated in this work. This transition, induced by the cationic surfactant dodecyltrimethylammonium chloride (DTAC), is accompanied by partial unfolding of the protein. In this work, unfolding of bovine beta-lactoglobulin in DTAC is compared with its unfolding induced by the chemical denaturant guanidine hydrochloride (GnHCl). The final protein states attained in the two media have quite different secondary structure: in DTAC the alpha-helical content increases, leading to the so-called alpha-state; in GnHCl the amount of ordered secondary-structure decreases, resulting in a random coil-rich final state (denatured, or D, state). To obtain information on both mechanistic routes, in DTAC and GnHCl, and to characterize intermediates, the kinetics of unfolding were investigated in the two media. Equilibrium and kinetic data show the partial accumulation of an on-pathway intermediate in each unfolding route: in DTAC, an intermediate (I-1) with mostly native secondary structure but loose tertiary structure appears between the native (beta) and alpha-states; in GnHCl, another intermediate (I-2) appears between states beta and D. Kinetic rate constants follow a linear Chevron-plot representation in GnHCl, but show a more complex mechanism in DTAC, which acts like a stronger binding species.
dc.description.versioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doi10.1529/biophysj.106.101667
dc.identifier.issn0006-3495
dc.identifier.urihttp://hdl.handle.net/10400.1/11811
dc.language.isoeng
dc.peerreviewedyes
dc.publisherBiophysical Soc
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectAlpha-helical structure
dc.subjectConformational transitions
dc.subjectCationic amphiphiles
dc.subjectCircular-dichroism
dc.subjectProtein
dc.subjectFluorescence
dc.subjectTrifluoroethanol
dc.subjectIntermediate
dc.subjectEquilibrium
dc.subjectAssociation
dc.titleUnfolding kinetics of beta-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage3612
oaire.citation.issue10
oaire.citation.startPage3601
oaire.citation.titleBiophysical Journal
oaire.citation.volume93
person.familyNamePinho Melo
person.givenNameEduardo
person.identifier1443188
person.identifier.ciencia-id3C1C-C10C-1510
person.identifier.orcid0000-0002-0974-8977
person.identifier.scopus-author-id35566177900
rcaap.rightsopenAccess
rcaap.typearticle
relation.isAuthorOfPublication5fa1895f-5577-4652-961a-886ec9bf41b1
relation.isAuthorOfPublication.latestForDiscovery5fa1895f-5577-4652-961a-886ec9bf41b1

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