Steric constraints as folding coadjuvant
Autor(a) principal: | |
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Data de Publicação: | 2003 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1103/PhysRevE.67.031901 http://hdl.handle.net/11449/227977 |
Resumo: | Through the analyses of the Miyazawa-Jernigan matrix it has been shown that the hydrophobic effect generates the dominant driving force for protein folding. By using both lattice and off-lattice models, it is shown that hydrophobic-type potentials are indeed efficient in inducing the chain through nativelike configurations, but they fail to provide sufficient stability so as to keep the chain in the native state. However, through comparative Monte Carlo simulations, it is shown that hydrophobic potentials and steric constraints are two basic ingredients for the folding process. Specifically, it is shown that suitable pairwise steric constraints introduce strong changes on the configurational activity, whose main consequence is a huge increase in the overall stability condition of the native state; detailed analysis of the effects of steric constraints on the heat capacity and configurational activity are provided. The present results support the view that the folding problem of globular proteins can be approached as a process in which the mechanism to reach the native conformation and the requirements for the globule stability are uncoupled. © 2003 The American Physical Society. |
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Repositório Institucional da UNESP |
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Steric constraints as folding coadjuvantThrough the analyses of the Miyazawa-Jernigan matrix it has been shown that the hydrophobic effect generates the dominant driving force for protein folding. By using both lattice and off-lattice models, it is shown that hydrophobic-type potentials are indeed efficient in inducing the chain through nativelike configurations, but they fail to provide sufficient stability so as to keep the chain in the native state. However, through comparative Monte Carlo simulations, it is shown that hydrophobic potentials and steric constraints are two basic ingredients for the folding process. Specifically, it is shown that suitable pairwise steric constraints introduce strong changes on the configurational activity, whose main consequence is a huge increase in the overall stability condition of the native state; detailed analysis of the effects of steric constraints on the heat capacity and configurational activity are provided. The present results support the view that the folding problem of globular proteins can be approached as a process in which the mechanism to reach the native conformation and the requirements for the globule stability are uncoupled. © 2003 The American Physical Society.Universidade de São Paulo FFCLRP Departamento de Física e Matemática, Avenida Bandeirantes, 3000, Ribeirão Preto, São Paulo, 14040.000Universidade Estadual Paulista IBILCE Departamento de Física, Rua Cristovão Colombo 2265, Jardim Nazareth, São José do Rio Preto, 15054-000Universidade de São Paulo FFCLRP Departamento de Física e Química, Avenida do Café S/N - Monte Alegre, Ribeirão Preto, São Paulo, 14040.903Universidade Estadual Paulista IBILCE Departamento de Física, Rua Cristovão Colombo 2265, Jardim Nazareth, São José do Rio Preto, 15054-000Universidade de São Paulo (USP)Universidade Estadual Paulista (UNESP)Tarragó, M. E.P.Rocha, Luiz F. O. [UNESP]daSilva, R. A.Caliri, A.2022-04-29T07:26:02Z2022-04-29T07:26:02Z2003-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article7http://dx.doi.org/10.1103/PhysRevE.67.031901Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics, v. 67, n. 3, p. 7-, 2003.1063-651Xhttp://hdl.handle.net/11449/22797710.1103/PhysRevE.67.0319012-s2.0-84930063841Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPhysical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topicsinfo:eu-repo/semantics/openAccess2022-04-29T07:26:02Zoai:repositorio.unesp.br:11449/227977Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:46:33.506249Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Steric constraints as folding coadjuvant |
title |
Steric constraints as folding coadjuvant |
spellingShingle |
Steric constraints as folding coadjuvant Tarragó, M. E.P. |
title_short |
Steric constraints as folding coadjuvant |
title_full |
Steric constraints as folding coadjuvant |
title_fullStr |
Steric constraints as folding coadjuvant |
title_full_unstemmed |
Steric constraints as folding coadjuvant |
title_sort |
Steric constraints as folding coadjuvant |
author |
Tarragó, M. E.P. |
author_facet |
Tarragó, M. E.P. Rocha, Luiz F. O. [UNESP] daSilva, R. A. Caliri, A. |
author_role |
author |
author2 |
Rocha, Luiz F. O. [UNESP] daSilva, R. A. Caliri, A. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Tarragó, M. E.P. Rocha, Luiz F. O. [UNESP] daSilva, R. A. Caliri, A. |
description |
Through the analyses of the Miyazawa-Jernigan matrix it has been shown that the hydrophobic effect generates the dominant driving force for protein folding. By using both lattice and off-lattice models, it is shown that hydrophobic-type potentials are indeed efficient in inducing the chain through nativelike configurations, but they fail to provide sufficient stability so as to keep the chain in the native state. However, through comparative Monte Carlo simulations, it is shown that hydrophobic potentials and steric constraints are two basic ingredients for the folding process. Specifically, it is shown that suitable pairwise steric constraints introduce strong changes on the configurational activity, whose main consequence is a huge increase in the overall stability condition of the native state; detailed analysis of the effects of steric constraints on the heat capacity and configurational activity are provided. The present results support the view that the folding problem of globular proteins can be approached as a process in which the mechanism to reach the native conformation and the requirements for the globule stability are uncoupled. © 2003 The American Physical Society. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-01-01 2022-04-29T07:26:02Z 2022-04-29T07:26:02Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1103/PhysRevE.67.031901 Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics, v. 67, n. 3, p. 7-, 2003. 1063-651X http://hdl.handle.net/11449/227977 10.1103/PhysRevE.67.031901 2-s2.0-84930063841 |
url |
http://dx.doi.org/10.1103/PhysRevE.67.031901 http://hdl.handle.net/11449/227977 |
identifier_str_mv |
Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics, v. 67, n. 3, p. 7-, 2003. 1063-651X 10.1103/PhysRevE.67.031901 2-s2.0-84930063841 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
7 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1808129550746386432 |