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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/29703
Ver los metadatos del registro completo
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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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1846781277848469504 |
score |
12.982451 |