Stability and folding studies of the N-domain of troponin C. Evidence for the formation of an intermediate

dc.creatorRamos, CHI
dc.creatorLima, MV
dc.creatorSilva, SLF
dc.creatorBorin, PFL
dc.creatorRegis, WCB
dc.creatorSantoro, MM
dc.date2004
dc.date42186
dc.date2014-11-18T00:07:30Z
dc.date2015-11-26T17:43:43Z
dc.date2014-11-18T00:07:30Z
dc.date2015-11-26T17:43:43Z
dc.date.accessioned2018-03-29T00:25:49Z
dc.date.available2018-03-29T00:25:49Z
dc.identifierArchives Of Biochemistry And Biophysics. Elsevier Science Inc, v. 427, n. 2, n. 135, n. 142, 2004.
dc.identifier0003-9861
dc.identifierWOS:000222324500002
dc.identifier10.1016/j.abb.2004.05.002
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/74453
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/74453
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/74453
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1287670
dc.descriptionWe report here on the stability and folding of the 91 residue alpha-helical F29W N-terminal domain of chicken skeletal muscle troponin C (TnC(1-91)F29W), the thin filament calcium-binding component. Unfolding was monitored by differential scanning calorimetry, circular dichroism, and intrinsic fluorescence spectroscopy using urea, pH, and temperature as denaturants, in the absence and in the presence of calcium. The unfolding of TnC(1-91)F29W was reversible and did not follow a two-state transition, suggesting that an intermediate may be present during this reaction. Our results support the hypothesis that intermediates are likely to occur during the folding of small proteins and domains. The physiological significance of the presence of an intermediate in the folding pathway of troponin C is discussed. (C) 2004 Elsevier Inc. All rights reserved.
dc.description427
dc.description2
dc.description135
dc.description142
dc.languageen
dc.publisherElsevier Science Inc
dc.publisherNew York
dc.publisherEUA
dc.relationArchives Of Biochemistry And Biophysics
dc.relationArch. Biochem. Biophys.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectprotein folding
dc.subjectfolding intermediate
dc.subjecttroponin C
dc.subjectspectroscopy
dc.subjectthermodynamic
dc.subjectmuscle contraction
dc.subjectcalcium binding
dc.subjectMolten-globule State
dc.subjectInduced Structural-changes
dc.subjectSkeletal-muscle
dc.subjectRegulatory Domains
dc.subjectLow-temperature
dc.subjectWild-type
dc.subjectProteins
dc.subjectBinding
dc.subjectPolymerase
dc.subjectResolution
dc.titleStability and folding studies of the N-domain of troponin C. Evidence for the formation of an intermediate
dc.typeArtículos de revistas


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