The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

Autores
Espinosa Silva, Yanis Ricardo; Caffarena, Ernesto Raúl; Grigera, Jose Raul
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An exciting debate arises when microscopic mechanisms involved in the denaturation of proteins at high pressures are explained. In particular, the issue emerges when the hydrophobic effect is invoked, given that hydrophobicity cannot elucidate by itself the volume changes measured during protein unfolding. In this work, we study by the use of molecular dynamics simulations and essential dynamics analysis the relation between the solvation dynamics, volume, and water structure when apomyoglobin is subjected to a hydrostatic pressure regime. Accordingly, the mechanism of cold denaturation of proteins under high-pressure can be related to the disruption of the hydrogen-bond network of water favoring the coexistence of two states, low-density and high-density water, which directly implies in the formation of a molten globule once the threshold of 200 MPa has been overcome.
Fil: Espinosa Silva, Yanis Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Caffarena, Ernesto Raúl. Ministerio de Salud de Brasil. Fundación Oswaldo Cruz. Programa de Computación Cientifica. Biofísica Computacional y Modelaje Molecular; Brasil
Fil: Grigera, Jose Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina
Materia
protein volume
Hydrostatic pressure
Hydrophobicity
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:11336/125855
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobinEspinosa Silva, Yanis RicardoCaffarena, Ernesto RaúlGrigera, Jose Raulprotein volumeHydrostatic pressureHydrophobicityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1An exciting debate arises when microscopic mechanisms involved in the denaturation of proteins at high pressures are explained. In particular, the issue emerges when the hydrophobic effect is invoked, given that hydrophobicity cannot elucidate by itself the volume changes measured during protein unfolding. In this work, we study by the use of molecular dynamics simulations and essential dynamics analysis the relation between the solvation dynamics, volume, and water structure when apomyoglobin is subjected to a hydrostatic pressure regime. Accordingly, the mechanism of cold denaturation of proteins under high-pressure can be related to the disruption of the hydrogen-bond network of water favoring the coexistence of two states, low-density and high-density water, which directly implies in the formation of a molten globule once the threshold of 200 MPa has been overcome.Fil: Espinosa Silva, Yanis Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Caffarena, Ernesto Raúl. Ministerio de Salud de Brasil. Fundación Oswaldo Cruz. Programa de Computación Cientifica. Biofísica Computacional y Modelaje Molecular; BrasilFil: Grigera, Jose Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; ArgentinaAmerican Institute of Physics2019-02-21info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/125855Espinosa Silva, Yanis Ricardo; Caffarena, Ernesto Raúl; Grigera, Jose Raul; The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin; American Institute of Physics; Journal of Chemical Physics; 150; 7; 21-2-2019; 1-100021-9606CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://aip.scitation.org/doi/10.1063/1.5080942info:eu-repo/semantics/altIdentifier/doi/10.1063/1.5080942info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:40:57Zoai:ri.conicet.gov.ar:11336/125855instacron: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:34982025-09-29 10:40:57.889CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
title The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
spellingShingle The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
Espinosa Silva, Yanis Ricardo
protein volume
Hydrostatic pressure
Hydrophobicity
title_short The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
title_full The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
title_fullStr The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
title_full_unstemmed The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
title_sort The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
dc.creator.none.fl_str_mv Espinosa Silva, Yanis Ricardo
Caffarena, Ernesto Raúl
Grigera, Jose Raul
author Espinosa Silva, Yanis Ricardo
author_facet Espinosa Silva, Yanis Ricardo
Caffarena, Ernesto Raúl
Grigera, Jose Raul
author_role author
author2 Caffarena, Ernesto Raúl
Grigera, Jose Raul
author2_role author
author
dc.subject.none.fl_str_mv protein volume
Hydrostatic pressure
Hydrophobicity
topic protein volume
Hydrostatic pressure
Hydrophobicity
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv An exciting debate arises when microscopic mechanisms involved in the denaturation of proteins at high pressures are explained. In particular, the issue emerges when the hydrophobic effect is invoked, given that hydrophobicity cannot elucidate by itself the volume changes measured during protein unfolding. In this work, we study by the use of molecular dynamics simulations and essential dynamics analysis the relation between the solvation dynamics, volume, and water structure when apomyoglobin is subjected to a hydrostatic pressure regime. Accordingly, the mechanism of cold denaturation of proteins under high-pressure can be related to the disruption of the hydrogen-bond network of water favoring the coexistence of two states, low-density and high-density water, which directly implies in the formation of a molten globule once the threshold of 200 MPa has been overcome.
Fil: Espinosa Silva, Yanis Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Caffarena, Ernesto Raúl. Ministerio de Salud de Brasil. Fundación Oswaldo Cruz. Programa de Computación Cientifica. Biofísica Computacional y Modelaje Molecular; Brasil
Fil: Grigera, Jose Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina
description An exciting debate arises when microscopic mechanisms involved in the denaturation of proteins at high pressures are explained. In particular, the issue emerges when the hydrophobic effect is invoked, given that hydrophobicity cannot elucidate by itself the volume changes measured during protein unfolding. In this work, we study by the use of molecular dynamics simulations and essential dynamics analysis the relation between the solvation dynamics, volume, and water structure when apomyoglobin is subjected to a hydrostatic pressure regime. Accordingly, the mechanism of cold denaturation of proteins under high-pressure can be related to the disruption of the hydrogen-bond network of water favoring the coexistence of two states, low-density and high-density water, which directly implies in the formation of a molten globule once the threshold of 200 MPa has been overcome.
publishDate 2019
dc.date.none.fl_str_mv 2019-02-21
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/11336/125855
Espinosa Silva, Yanis Ricardo; Caffarena, Ernesto Raúl; Grigera, Jose Raul; The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin; American Institute of Physics; Journal of Chemical Physics; 150; 7; 21-2-2019; 1-10
0021-9606
CONICET Digital
CONICET
url http://hdl.handle.net/11336/125855
identifier_str_mv Espinosa Silva, Yanis Ricardo; Caffarena, Ernesto Raúl; Grigera, Jose Raul; The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin; American Institute of Physics; Journal of Chemical Physics; 150; 7; 21-2-2019; 1-10
0021-9606
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://aip.scitation.org/doi/10.1063/1.5080942
info:eu-repo/semantics/altIdentifier/doi/10.1063/1.5080942
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
application/pdf
dc.publisher.none.fl_str_mv American Institute of Physics
publisher.none.fl_str_mv American Institute of Physics
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 13.070432

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