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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleIs there nascent structure in the intrinsically disordered region of troponin I?pt_BR
dc.contributor.authorJulien, Opt_BR
dc.contributor.authorMercier, Ppt_BR
dc.contributor.authorAllen, CNpt_BR
dc.contributor.authorFisette, Opt_BR
dc.contributor.authorRamos, CHIpt_BR
dc.contributor.authorLague, Ppt_BR
dc.contributor.authorBlumenschein, TMApt_BR
dc.contributor.authorSykes, BDpt_BR
unicamp.author.emailbrian.sykes@ualberta.capt_BR
unicamp.authorJulien, Olivier Mercier, Pascal Sykes, Brian D. Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canadapt_BR
unicamp.authorAllen, Claire N. Blumenschein, Tharin M. A. Univ E Anglia, Sch Chem, Norwich NR4 7TJ, Norfolk, Englandpt_BR
unicamp.authorFisette, Olivier Laguee, Patrick Univ Laval, Dept Biochim & Microbiol, Quebec City, PQ, Canadapt_BR
unicamp.authorRamos, Carlos H. I. Univ Estadual Campinas, Inst Chem, Campinas, SP, Brazilpt_BR
dc.subjectNMRpt_BR
dc.subjectmuscle regulationpt_BR
dc.subjectprotein dynamicspt_BR
dc.subjectmolecular dynamicspt_BR
dc.subjectNMR relaxationpt_BR
dc.subject.wosHuman Cardiac Troponinpt_BR
dc.subject.wosRegulatory Domainpt_BR
dc.subject.wosStriated-musclept_BR
dc.subject.wosDynamicspt_BR
dc.subject.wosProteinpt_BR
dc.subject.wosComplexpt_BR
dc.subject.wosContractionpt_BR
dc.subject.wosBackbonept_BR
dc.subject.wosRelaxationpt_BR
dc.subject.wosMutationspt_BR
dc.description.abstractIn striated muscle, the binding of calcium to troponin C (TnC) results in the removal of the C-terminal region of the inhibitory protein troponin I (TnI) from actin. While structural studies of the muscle system have been successful in determining the overall organization of most of the components involved in force generation at the atomic level, the structure and dynamics of the C-terminal region of TnI remains controversial. This domain of TnI is highly flexible, and it has been proposed that this intrinsically disordered region (IDR) regulates contraction via a "fly-casting'' mechanism. Different structures have been presented for this region using different methodologies: a single alpha-helix, a "mobile domain'' containing a small beta-sheet, an unstructured region, and a two helix segment. To investigate whether this IDR has in fact any nascent structure, we have constructed a skeletal TnC-TnI chimera that contains the N-domain of TnC (1-90), a short linker (GGAGG), and the C-terminal region of TnI (97-182) and have acquired (15)N NMR relaxation data for this chimera. We compare the experimental relaxation parameters with those calculated from molecular dynamic simulations using four models based upon the structural studies. Our experimental results suggest that the C-terminal region of TnI does not contain any defined secondary structure, supporting the "fly-casting'' mechanism. We interpret the presence of a "plateau'' in the (15)N NMR relaxation data as being an intrinsic property of IDRs. We also identified a more rigid adjacent region of TnI that has implications for muscle performance under ischemic conditions.pt
dc.relation.ispartofProteins-structure Function And Bioinformaticspt_BR
dc.relation.ispartofabbreviationProteinspt_BR
dc.publisher.cityMaldenpt_BR
dc.publisher.countryEUApt_BR
dc.publisherWiley-blackwellpt_BR
dc.date.issued2011pt_BR
dc.date.monthofcirculationAPRpt_BR
dc.identifier.citationProteins-structure Function And Bioinformatics. Wiley-blackwell, v. 79, n. 4, n. 1240, n. 1250, 2011.pt_BR
dc.language.isoenpt_BR
dc.description.volume79pt_BR
dc.description.issuenumber4pt_BR
dc.description.firstpage1240pt_BR
dc.description.lastpage1250pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.htmlpt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0887-3585pt_BR
dc.identifier.wosidWOS:000288138700017pt_BR
dc.identifier.doi10.1002/prot.22959pt_BR
dc.description.sponsorshipWolfson Foundationpt_BR
dc.description.sponsorshipCanadian Institutes of Health Research (CIHR)pt_BR
dc.description.sponsorshipNANUCpt_BR
dc.description.sponsorshipNatural Science and Engineering Research Council of Canada (NSERC)pt_BR
dc.description.sponsorshipAlberta Heritage Foundation for Medical Research (AHFMR)pt_BR
dc.date.available2014-07-30T14:35:28Z
dc.date.available2015-11-26T16:37:31Z-
dc.date.accessioned2014-07-30T14:35:28Z
dc.date.accessioned2015-11-26T16:37:31Z-
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dc.description.provenanceMade available in DSpace on 2015-11-26T16:37:31Z (GMT). No. of bitstreams: 2 WOS000288138700017.pdf: 3245342 bytes, checksum: 1b2856f2a720f3b1077006edad5d2868 (MD5) WOS000288138700017.pdf.txt: 42512 bytes, checksum: 1a1f3525f94db23fb19e46c97ad0e5eb (MD5) Previous issue date: 2011en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60773
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60773-
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