Long-Range Correlated Dynamics in Intrinsically Disordered Proteins

Autores
Parigi, Giacomo; Rezaei Ghaleh, Nasrollah; Giachetti, Andrea; Becker, Stefan; Fernandez, Claudio Oscar; Blackledger, Martin; Griesinger, Christian; Zweckstetter, Markus; Luchinat, Claudio
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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
Fil: Parigi, Giacomo. University of Florence; Italia
Fil: Rezaei Ghaleh, Nasrollah. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania
Fil: Giachetti, Andrea. University of Florence; Italia
Fil: Becker, Stefan. Max Planck Institute for Biophysical Chemistry; Alemania
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
Fil: Blackledger, Martin. Institut de Biologie Structurale; Francia
Fil: Griesinger, Christian. Max Planck Institute for Biophysical Chemistry; Alemania
Fil: Zweckstetter, Markus. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania. University Medical Center; Alemania
Fil: Luchinat, Claudio. University of Florence; Italia
Materia
Proteinas Intrinsicamente Desordenadas
Dinamica
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/29703

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spelling Long-Range Correlated Dynamics in Intrinsically Disordered ProteinsParigi, GiacomoRezaei Ghaleh, NasrollahGiachetti, AndreaBecker, StefanFernandez, Claudio OscarBlackledger, MartinGriesinger, ChristianZweckstetter, MarkusLuchinat, ClaudioProteinas Intrinsicamente DesordenadasDinamicahttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Intrinsically 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 systemsFil: Parigi, Giacomo. University of Florence; ItaliaFil: Rezaei Ghaleh, Nasrollah. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; AlemaniaFil: Giachetti, Andrea. University of Florence; ItaliaFil: Becker, Stefan. Max Planck Institute for Biophysical Chemistry; AlemaniaFil: 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; ArgentinaFil: Blackledger, Martin. Institut de Biologie Structurale; FranciaFil: Griesinger, Christian. Max Planck Institute for Biophysical Chemistry; AlemaniaFil: Zweckstetter, Markus. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania. University Medical Center; AlemaniaFil: Luchinat, Claudio. University of Florence; ItaliaAmerican Chemical Society2014-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29703Parigi, 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; 16201-162090002-7863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/ja506820rinfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/ja506820rinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:03:46Zoai:ri.conicet.gov.ar:11336/29703instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:03:46.37CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
title Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
spellingShingle Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
Parigi, Giacomo
Proteinas Intrinsicamente Desordenadas
Dinamica
title_short Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
title_full Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
title_fullStr Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
title_full_unstemmed Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
title_sort Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
dc.creator.none.fl_str_mv Parigi, Giacomo
Rezaei Ghaleh, Nasrollah
Giachetti, Andrea
Becker, Stefan
Fernandez, Claudio Oscar
Blackledger, Martin
Griesinger, Christian
Zweckstetter, Markus
Luchinat, Claudio
author Parigi, Giacomo
author_facet Parigi, Giacomo
Rezaei Ghaleh, Nasrollah
Giachetti, Andrea
Becker, Stefan
Fernandez, Claudio Oscar
Blackledger, Martin
Griesinger, Christian
Zweckstetter, Markus
Luchinat, Claudio
author_role author
author2 Rezaei Ghaleh, Nasrollah
Giachetti, Andrea
Becker, Stefan
Fernandez, Claudio Oscar
Blackledger, Martin
Griesinger, Christian
Zweckstetter, Markus
Luchinat, Claudio
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Proteinas Intrinsicamente Desordenadas
Dinamica
topic Proteinas Intrinsicamente Desordenadas
Dinamica
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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
Fil: Parigi, Giacomo. University of Florence; Italia
Fil: Rezaei Ghaleh, Nasrollah. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania
Fil: Giachetti, Andrea. University of Florence; Italia
Fil: Becker, Stefan. Max Planck Institute for Biophysical Chemistry; Alemania
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
Fil: Blackledger, Martin. Institut de Biologie Structurale; Francia
Fil: Griesinger, Christian. Max Planck Institute for Biophysical Chemistry; Alemania
Fil: Zweckstetter, Markus. German Center for Neurodegenerative Diseases; Alemania. Max Planck Institute for Biophysical Chemistry; Alemania. University Medical Center; Alemania
Fil: Luchinat, Claudio. University of Florence; Italia
description 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
publishDate 2014
dc.date.none.fl_str_mv 2014-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/29703
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
0002-7863
CONICET Digital
CONICET
url http://hdl.handle.net/11336/29703
identifier_str_mv 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
0002-7863
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/ja506820r
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/ja506820r
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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