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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/72838
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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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1842269269741535232 |
score |
13.13397 |