Critical Fluctuations in the Native State of Proteins

Autores
Tang, Qian Yuan; Zhang, Yang Yang; Wang, Jun; Wang, Wei; Chialvo, Dante Renato
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to the protein sizes. The scaling relations between the correlations or susceptibility and protein sizes resemble those in other physical and biological systems near their critical points. These results indicate that, at the native states, motions of each residue are felt by every other one in the protein. We also find that proteins with larger susceptibility are more frequently observed in nature. Overall, our results suggest that the protein's native state is critical.
Fil: Tang, Qian Yuan. Nanjing University; China
Fil: Zhang, Yang Yang. Nanjing University; China
Fil: Wang, Jun. Nanjing University; China
Fil: Wang, Wei. Nanjing University; China
Fil: Chialvo, Dante Renato. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Proteins
Critical Phenomena
Finite-Size Scaling
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:11336/72838

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network_name_str CONICET Digital (CONICET)
spelling Critical Fluctuations in the Native State of ProteinsTang, Qian YuanZhang, Yang YangWang, JunWang, WeiChialvo, Dante RenatoProteinsCritical PhenomenaFinite-Size Scalinghttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to the protein sizes. The scaling relations between the correlations or susceptibility and protein sizes resemble those in other physical and biological systems near their critical points. These results indicate that, at the native states, motions of each residue are felt by every other one in the protein. We also find that proteins with larger susceptibility are more frequently observed in nature. Overall, our results suggest that the protein's native state is critical.Fil: Tang, Qian Yuan. Nanjing University; ChinaFil: Zhang, Yang Yang. Nanjing University; ChinaFil: Wang, Jun. Nanjing University; ChinaFil: Wang, Wei. Nanjing University; ChinaFil: Chialvo, Dante Renato. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAmerican Physical Society2017-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/72838Tang, Qian Yuan; Zhang, Yang Yang; Wang, Jun; Wang, Wei; Chialvo, Dante Renato; Critical Fluctuations in the Native State of Proteins; American Physical Society; Physical Review Letters; 118; 8; 2-2017; 1-5; 0881020031-9007CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1103/PhysRevLett.118.088102info:eu-repo/semantics/altIdentifier/url/https://journals.aps.org/prl/abstract/10.1103/PhysRevLett.118.088102info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:54:10Zoai:ri.conicet.gov.ar:11336/72838instacron: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:34982025-09-03 09:54:10.728CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Critical Fluctuations in the Native State of Proteins
title Critical Fluctuations in the Native State of Proteins
spellingShingle Critical Fluctuations in the Native State of Proteins
Tang, Qian Yuan
Proteins
Critical Phenomena
Finite-Size Scaling
title_short Critical Fluctuations in the Native State of Proteins
title_full Critical Fluctuations in the Native State of Proteins
title_fullStr Critical Fluctuations in the Native State of Proteins
title_full_unstemmed Critical Fluctuations in the Native State of Proteins
title_sort Critical Fluctuations in the Native State of Proteins
dc.creator.none.fl_str_mv Tang, Qian Yuan
Zhang, Yang Yang
Wang, Jun
Wang, Wei
Chialvo, Dante Renato
author Tang, Qian Yuan
author_facet Tang, Qian Yuan
Zhang, Yang Yang
Wang, Jun
Wang, Wei
Chialvo, Dante Renato
author_role author
author2 Zhang, Yang Yang
Wang, Jun
Wang, Wei
Chialvo, Dante Renato
author2_role author
author
author
author
dc.subject.none.fl_str_mv Proteins
Critical Phenomena
Finite-Size Scaling
topic Proteins
Critical Phenomena
Finite-Size Scaling
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to the protein sizes. The scaling relations between the correlations or susceptibility and protein sizes resemble those in other physical and biological systems near their critical points. These results indicate that, at the native states, motions of each residue are felt by every other one in the protein. We also find that proteins with larger susceptibility are more frequently observed in nature. Overall, our results suggest that the protein's native state is critical.
Fil: Tang, Qian Yuan. Nanjing University; China
Fil: Zhang, Yang Yang. Nanjing University; China
Fil: Wang, Jun. Nanjing University; China
Fil: Wang, Wei. Nanjing University; China
Fil: Chialvo, Dante Renato. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to the protein sizes. The scaling relations between the correlations or susceptibility and protein sizes resemble those in other physical and biological systems near their critical points. These results indicate that, at the native states, motions of each residue are felt by every other one in the protein. We also find that proteins with larger susceptibility are more frequently observed in nature. Overall, our results suggest that the protein's native state is critical.
publishDate 2017
dc.date.none.fl_str_mv 2017-02
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/11336/72838
Tang, Qian Yuan; Zhang, Yang Yang; Wang, Jun; Wang, Wei; Chialvo, Dante Renato; Critical Fluctuations in the Native State of Proteins; American Physical Society; Physical Review Letters; 118; 8; 2-2017; 1-5; 088102
0031-9007
CONICET Digital
CONICET
url http://hdl.handle.net/11336/72838
identifier_str_mv Tang, Qian Yuan; Zhang, Yang Yang; Wang, Jun; Wang, Wei; Chialvo, Dante Renato; Critical Fluctuations in the Native State of Proteins; American Physical Society; Physical Review Letters; 118; 8; 2-2017; 1-5; 088102
0031-9007
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1103/PhysRevLett.118.088102
info:eu-repo/semantics/altIdentifier/url/https://journals.aps.org/prl/abstract/10.1103/PhysRevLett.118.088102
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 Physical Society
publisher.none.fl_str_mv American Physical 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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score 13.13397