Is there nascent structure in the intrinsically disordered region of troponin I?

dc.creatorJulien, O
dc.creatorMercier, P
dc.creatorAllen, CN
dc.creatorFisette, O
dc.creatorRamos, CHI
dc.creatorLague, P
dc.creatorBlumenschein, TMA
dc.creatorSykes, BD
dc.date2011
dc.dateAPR
dc.date2014-07-30T14:35:28Z
dc.date2015-11-26T16:37:31Z
dc.date2014-07-30T14:35:28Z
dc.date2015-11-26T16:37:31Z
dc.date.accessioned2018-03-28T23:20:38Z
dc.date.available2018-03-28T23:20:38Z
dc.identifierProteins-structure Function And Bioinformatics. Wiley-blackwell, v. 79, n. 4, n. 1240, n. 1250, 2011.
dc.identifier0887-3585
dc.identifierWOS:000288138700017
dc.identifier10.1002/prot.22959
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60773
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60773
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1272042
dc.descriptionIn 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.
dc.description79
dc.description4
dc.description1240
dc.description1250
dc.descriptionWolfson Foundation
dc.descriptionCanadian Institutes of Health Research (CIHR)
dc.descriptionNANUC
dc.descriptionNatural Science and Engineering Research Council of Canada (NSERC)
dc.descriptionAlberta Heritage Foundation for Medical Research (AHFMR)
dc.languageen
dc.publisherWiley-blackwell
dc.publisherMalden
dc.publisherEUA
dc.relationProteins-structure Function And Bioinformatics
dc.relationProteins
dc.rightsfechado
dc.rightshttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.sourceWeb of Science
dc.subjectNMR
dc.subjectmuscle regulation
dc.subjectprotein dynamics
dc.subjectmolecular dynamics
dc.subjectNMR relaxation
dc.subjectHuman Cardiac Troponin
dc.subjectRegulatory Domain
dc.subjectStriated-muscle
dc.subjectDynamics
dc.subjectProtein
dc.subjectComplex
dc.subjectContraction
dc.subjectBackbone
dc.subjectRelaxation
dc.subjectMutations
dc.titleIs there nascent structure in the intrinsically disordered region of troponin I?
dc.typeArtículos de revistas


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