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dc.contributor.author
Parigi, Giacomo
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dc.contributor.author
Rezaei Ghaleh, Nasrollah
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dc.contributor.author
Giachetti, Andrea
dc.contributor.author
Becker, Stefan
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dc.contributor.author
Fernandez, Claudio Oscar
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dc.contributor.author
Blackledger, Martin
dc.contributor.author
Griesinger, Christian
dc.contributor.author
Zweckstetter, Markus
dc.contributor.author
Luchinat, Claudio
dc.date.available
2017-12-05T15:10:59Z
dc.date.issued
2014-10
dc.identifier.citation
Parigi, 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.identifier.issn
0002-7863
dc.identifier.uri
http://hdl.handle.net/11336/29703
dc.description.abstract
Intrinsically 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.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Proteinas Intrinsicamente Desordenadas
dc.subject
Dinamica
dc.subject.classification
Otras Ciencias Químicas
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dc.subject.classification
Ciencias Químicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-12-04T19:16:18Z
dc.journal.volume
136
dc.journal.pagination
16201-16209
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Washington
dc.description.fil
Fil: Parigi, Giacomo. University of Florence; Italia
dc.description.fil
Fil: Rezaei Ghaleh, Nasrollah. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania
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Fil: Giachetti, Andrea. University of Florence; Italia
dc.description.fil
Fil: Becker, Stefan. Max Planck Institute for Biophysical Chemistry; Alemania
dc.description.fil
Fil: 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
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Fil: Blackledger, Martin. Institut de Biologie Structurale; Francia
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Fil: Griesinger, Christian. Max Planck Institute for Biophysical Chemistry; Alemania
dc.description.fil
Fil: Zweckstetter, Markus. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania. University Medical Center; Alemania
dc.description.fil
Fil: Luchinat, Claudio. University of Florence; Italia
dc.journal.title
Journal of the American Chemical Society
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/ja506820r
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/ja506820r
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