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dc.contributor.author
Espinosa Silva, Yanis Ricardo
dc.contributor.author
Caffarena, Ernesto Raúl
dc.contributor.author
Grigera, Jose Raul
dc.date.available
2021-02-17T19:54:32Z
dc.date.issued
2019-02-21
dc.identifier.citation
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
dc.identifier.issn
0021-9606
dc.identifier.uri
http://hdl.handle.net/11336/125855
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Institute of Physics
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
protein volume
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Hydrostatic pressure
dc.subject
Hydrophobicity
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Biofísica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-19T22:01:08Z
dc.journal.volume
150
dc.journal.number
7
dc.journal.pagination
1-10
dc.journal.pais
Estados Unidos
dc.description.fil
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
dc.description.fil
Fil: Caffarena, Ernesto Raúl. Ministerio de Salud de Brasil. Fundación Oswaldo Cruz. Programa de Computación Cientifica. Biofísica Computacional y Modelaje Molecular; Brasil
dc.description.fil
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
dc.journal.title
Journal of Chemical Physics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://aip.scitation.org/doi/10.1063/1.5080942
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1063/1.5080942
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