Nanoscale electrostatic theory of epistructural fields at the water-protein interface

Autores
Fernandez, Ariel
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Nanoscale solvent confinement at the protein-water interface promotes dipole orientations that are not aligned with the internal electrostatic field of a protein, yielding what we term epistructural polarization. To quantify this effect, an equation is derived from first principles relating epistructural polarization with the magnitude of local distortions in water coordination causative of interfacial tension. The equation defines a nanoscale electrostatic model of water and enables an estimation of protein denaturation free energies and the inference of hot spots for protein associations. The theoretical results are validated vis-à-vis calorimetric data, revealing the destabilizing effect of epistructural polarization and its molecular origin.
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática Alberto Calderon; Argentina. Collegium Basilea; Suiza
Materia
Nanotechnology
Molecular Biophysics
Nanodielectrics
Dehydron
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:11336/18931
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/18931
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network_name_str CONICET Digital (CONICET)
spelling Nanoscale electrostatic theory of epistructural fields at the water-protein interfaceFernandez, ArielNanotechnologyMolecular BiophysicsNanodielectricsDehydronhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1Nanoscale solvent confinement at the protein-water interface promotes dipole orientations that are not aligned with the internal electrostatic field of a protein, yielding what we term epistructural polarization. To quantify this effect, an equation is derived from first principles relating epistructural polarization with the magnitude of local distortions in water coordination causative of interfacial tension. The equation defines a nanoscale electrostatic model of water and enables an estimation of protein denaturation free energies and the inference of hot spots for protein associations. The theoretical results are validated vis-à-vis calorimetric data, revealing the destabilizing effect of epistructural polarization and its molecular origin.Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática Alberto Calderon; Argentina. Collegium Basilea; SuizaAmerican Institute of Physics2012-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/18931Fernandez, Ariel; Nanoscale electrostatic theory of epistructural fields at the water-protein interface; American Institute of Physics; Journal of Chemical Physics; 137; 23; 12-2012; 231101-2311010021-9606CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://aip.scitation.org/doi/10.1063/1.4772603info:eu-repo/semantics/altIdentifier/doi/10.1063/1.4772603info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:44:03Zoai:ri.conicet.gov.ar:11336/18931instacron: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 09:44:04.18CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nanoscale electrostatic theory of epistructural fields at the water-protein interface
title Nanoscale electrostatic theory of epistructural fields at the water-protein interface
spellingShingle Nanoscale electrostatic theory of epistructural fields at the water-protein interface
Fernandez, Ariel
Nanotechnology
Molecular Biophysics
Nanodielectrics
Dehydron
title_short Nanoscale electrostatic theory of epistructural fields at the water-protein interface
title_full Nanoscale electrostatic theory of epistructural fields at the water-protein interface
title_fullStr Nanoscale electrostatic theory of epistructural fields at the water-protein interface
title_full_unstemmed Nanoscale electrostatic theory of epistructural fields at the water-protein interface
title_sort Nanoscale electrostatic theory of epistructural fields at the water-protein interface
dc.creator.none.fl_str_mv Fernandez, Ariel
author Fernandez, Ariel
author_facet Fernandez, Ariel
author_role author
dc.subject.none.fl_str_mv Nanotechnology
Molecular Biophysics
Nanodielectrics
Dehydron
topic Nanotechnology
Molecular Biophysics
Nanodielectrics
Dehydron
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Nanoscale solvent confinement at the protein-water interface promotes dipole orientations that are not aligned with the internal electrostatic field of a protein, yielding what we term epistructural polarization. To quantify this effect, an equation is derived from first principles relating epistructural polarization with the magnitude of local distortions in water coordination causative of interfacial tension. The equation defines a nanoscale electrostatic model of water and enables an estimation of protein denaturation free energies and the inference of hot spots for protein associations. The theoretical results are validated vis-à-vis calorimetric data, revealing the destabilizing effect of epistructural polarization and its molecular origin.
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática Alberto Calderon; Argentina. Collegium Basilea; Suiza
description Nanoscale solvent confinement at the protein-water interface promotes dipole orientations that are not aligned with the internal electrostatic field of a protein, yielding what we term epistructural polarization. To quantify this effect, an equation is derived from first principles relating epistructural polarization with the magnitude of local distortions in water coordination causative of interfacial tension. The equation defines a nanoscale electrostatic model of water and enables an estimation of protein denaturation free energies and the inference of hot spots for protein associations. The theoretical results are validated vis-à-vis calorimetric data, revealing the destabilizing effect of epistructural polarization and its molecular origin.
publishDate 2012
dc.date.none.fl_str_mv 2012-12
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/11336/18931
Fernandez, Ariel; Nanoscale electrostatic theory of epistructural fields at the water-protein interface; American Institute of Physics; Journal of Chemical Physics; 137; 23; 12-2012; 231101-231101
0021-9606
CONICET Digital
CONICET
url http://hdl.handle.net/11336/18931
identifier_str_mv Fernandez, Ariel; Nanoscale electrostatic theory of epistructural fields at the water-protein interface; American Institute of Physics; Journal of Chemical Physics; 137; 23; 12-2012; 231101-231101
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/10.1063/1.4772603
info:eu-repo/semantics/altIdentifier/doi/10.1063/1.4772603
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 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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