The behavior of the hydrophobic effect under pressure and protein denaturation

Autores
Grigera, José Raúl; McCarthy, Andrés Norman
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of the effect of high pressure on globular proteins, such as lysozyme and apomyoglobin, we have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic effect that is known to be the main driving force in protein folding.
Facultad de Ciencias Exactas
Materia
Física
Proteína
Interacciones Hidrofóbicas e Hidrofílicas
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/82432
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/82432
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling The behavior of the hydrophobic effect under pressure and protein denaturationGrigera, José RaúlMcCarthy, Andrés NormanFísicaProteínaInteracciones Hidrofóbicas e HidrofílicasIt is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of the effect of high pressure on globular proteins, such as lysozyme and apomyoglobin, we have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic effect that is known to be the main driving force in protein folding.Facultad de Ciencias Exactas2010info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1626-1631http://sedici.unlp.edu.ar/handle/10915/82432enginfo:eu-repo/semantics/altIdentifier/issn/0006-3495info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2009.12.4298info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:47:47Zoai:sedici.unlp.edu.ar:10915/82432Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:47:47.223SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv The behavior of the hydrophobic effect under pressure and protein denaturation
title The behavior of the hydrophobic effect under pressure and protein denaturation
spellingShingle The behavior of the hydrophobic effect under pressure and protein denaturation
Grigera, José Raúl
Física
Proteína
Interacciones Hidrofóbicas e Hidrofílicas
title_short The behavior of the hydrophobic effect under pressure and protein denaturation
title_full The behavior of the hydrophobic effect under pressure and protein denaturation
title_fullStr The behavior of the hydrophobic effect under pressure and protein denaturation
title_full_unstemmed The behavior of the hydrophobic effect under pressure and protein denaturation
title_sort The behavior of the hydrophobic effect under pressure and protein denaturation
dc.creator.none.fl_str_mv Grigera, José Raúl
McCarthy, Andrés Norman
author Grigera, José Raúl
author_facet Grigera, José Raúl
McCarthy, Andrés Norman
author_role author
author2 McCarthy, Andrés Norman
author2_role author
dc.subject.none.fl_str_mv Física
Proteína
Interacciones Hidrofóbicas e Hidrofílicas
topic Física
Proteína
Interacciones Hidrofóbicas e Hidrofílicas
dc.description.none.fl_txt_mv It is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of the effect of high pressure on globular proteins, such as lysozyme and apomyoglobin, we have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic effect that is known to be the main driving force in protein folding.
Facultad de Ciencias Exactas
description It is well known that proteins denature under high pressure. The mechanism that underlies such a process is still not clearly understood, however, giving way to controversial interpretations. Using molecular dynamics simulation on systems that may be regarded experimentally as limiting examples of the effect of high pressure on globular proteins, such as lysozyme and apomyoglobin, we have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic effect that is known to be the main driving force in protein folding.
publishDate 2010
dc.date.none.fl_str_mv 2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/82432
url http://sedici.unlp.edu.ar/handle/10915/82432
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0006-3495
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2009.12.4298
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
1626-1631
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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