Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

Autores
Rossetti, German; Musiani, F.; Abad, E.; Dibenedetto, D.; Mouhib, H.; Fernandez, Claudio Oscar; Carloni, P.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Fil: Rossetti, German. Forschungszentrum Jülich; Alemania. Rwth Aachen University; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Musiani, F.. Forschungszentrum Jülich; Alemania. Scuola Internazionale Superiore di Studi Avanzati; Italia. Università di Bologna; Italia
Fil: Abad, E.. Forschungszentrum Jülich; Alemania
Fil: Dibenedetto, D.. Forschungszentrum Jülich; Alemania
Fil: Mouhib, H.. Rwth Aachen University; Alemania
Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina
Fil: Carloni, P.. Forschungszentrum Jülich; Alemania
Materia
synuclein
molecular dynamics
native structure
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:11336/52380
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Conformational ensemble of human α-synuclein physiological form predicted by molecular simulationsRossetti, GermanMusiani, F.Abad, E.Dibenedetto, D.Mouhib, H.Fernandez, Claudio OscarCarloni, P.synucleinmolecular dynamicsnative structurehttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.Fil: Rossetti, German. Forschungszentrum Jülich; Alemania. Rwth Aachen University; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Musiani, F.. Forschungszentrum Jülich; Alemania. Scuola Internazionale Superiore di Studi Avanzati; Italia. Università di Bologna; ItaliaFil: Abad, E.. Forschungszentrum Jülich; AlemaniaFil: Dibenedetto, D.. Forschungszentrum Jülich; AlemaniaFil: Mouhib, H.. Rwth Aachen University; AlemaniaFil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; ArgentinaFil: Carloni, P.. Forschungszentrum Jülich; AlemaniaRoyal Society of Chemistry2016-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/52380Rossetti, German; Musiani, F.; Abad, E.; Dibenedetto, D.; Mouhib, H.; et al.; Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 18; 8; 1-2016; 5702-57061463-9076CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1039/C5CP04549Einfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2016/CP/C5CP04549Einfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:42:20Zoai:ri.conicet.gov.ar:11336/52380instacron: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:34982025-11-12 09:42:21.045CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
title Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
spellingShingle Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
Rossetti, German
synuclein
molecular dynamics
native structure
title_short Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
title_full Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
title_fullStr Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
title_full_unstemmed Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
title_sort Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
dc.creator.none.fl_str_mv Rossetti, German
Musiani, F.
Abad, E.
Dibenedetto, D.
Mouhib, H.
Fernandez, Claudio Oscar
Carloni, P.
author Rossetti, German
author_facet Rossetti, German
Musiani, F.
Abad, E.
Dibenedetto, D.
Mouhib, H.
Fernandez, Claudio Oscar
Carloni, P.
author_role author
author2 Musiani, F.
Abad, E.
Dibenedetto, D.
Mouhib, H.
Fernandez, Claudio Oscar
Carloni, P.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv synuclein
molecular dynamics
native structure
topic synuclein
molecular dynamics
native structure
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Fil: Rossetti, German. Forschungszentrum Jülich; Alemania. Rwth Aachen University; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Musiani, F.. Forschungszentrum Jülich; Alemania. Scuola Internazionale Superiore di Studi Avanzati; Italia. Università di Bologna; Italia
Fil: Abad, E.. Forschungszentrum Jülich; Alemania
Fil: Dibenedetto, D.. Forschungszentrum Jülich; Alemania
Fil: Mouhib, H.. Rwth Aachen University; Alemania
Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina
Fil: Carloni, P.. Forschungszentrum Jülich; Alemania
description We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
publishDate 2016
dc.date.none.fl_str_mv 2016-01
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/11336/52380
Rossetti, German; Musiani, F.; Abad, E.; Dibenedetto, D.; Mouhib, H.; et al.; Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 18; 8; 1-2016; 5702-5706
1463-9076
CONICET Digital
CONICET
url http://hdl.handle.net/11336/52380
identifier_str_mv Rossetti, German; Musiani, F.; Abad, E.; Dibenedetto, D.; Mouhib, H.; et al.; Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations; Royal Society of Chemistry; Physical Chemistry Chemical Physics; 18; 8; 1-2016; 5702-5706
1463-9076
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1039/C5CP04549E
info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2016/CP/C5CP04549E
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 Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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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score 13.24909

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