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dc.creatorParigi, Giacomo-
dc.creatorRezaei Ghaleh, Nasrollah-
dc.creatorGiachetti, Andrea-
dc.creatorBecker, Stefan-
dc.creatorFernandez, Claudio Oscar-
dc.creatorBlackledger, Martin-
dc.creatorGriesinger, Christian-
dc.creatorZweckstetter, Markus-
dc.creatorLuchinat, Claudio-
dc.date2017-12-05T15:10:59Z-
dc.date2017-12-05T15:10:59Z-
dc.date2014-10-
dc.date2017-12-04T19:16:18Z-
dc.date.accessioned2019-04-29T15:39:43Z-
dc.date.available2019-04-29T15:39:43Z-
dc.date.issued2014-10-
dc.identifierParigi, Giacomo; Rezaei Ghaleh, Nasrollah; Giachetti, Andrea; Becker, Stefan; Fernandez, Claudio Oscar; et al.; Long-Range Correlated Dynamics in Intrinsically Disordered Proteins; American Chemical Society; Journal of the American Chemical Society; 136; 10-2014; 16201-16209-
dc.identifier0002-7863-
dc.identifierhttp://hdl.handle.net/11336/29703-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298861-
dc.descriptionIntrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in α-synuclein, which are related to genetic forms of Parkinson’s disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems-
dc.descriptionFil: Parigi, Giacomo. University of Florence; Italia-
dc.descriptionFil: Rezaei Ghaleh, Nasrollah. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania-
dc.descriptionFil: Giachetti, Andrea. University of Florence; Italia-
dc.descriptionFil: Becker, Stefan. Max Planck Institute for Biophysical Chemistry; Alemania-
dc.descriptionFil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones Para El Descubrimiento de Farmacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones Para El Descubrimiento de Farmacos de Rosario; Argentina-
dc.descriptionFil: Blackledger, Martin. Institut de Biologie Structurale; Francia-
dc.descriptionFil: Griesinger, Christian. Max Planck Institute for Biophysical Chemistry; Alemania-
dc.descriptionFil: Zweckstetter, Markus. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania. University Medical Center; Alemania-
dc.descriptionFil: Luchinat, Claudio. University of Florence; Italia-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherAmerican Chemical Society-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/ja506820r-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/ja506820r-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/46278-
dc.subjectproteinas intrinsicamente desordenadas-
dc.subjectdinamica-
dc.subjectOtras Ciencias Químicas-
dc.subjectCiencias Químicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleLong-Range Correlated Dynamics in Intrinsically Disordered Proteins-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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