Water promotes the sealing of nanoscale packing defects in folding proteins

Autores
Fernandez, Ariel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A net dipole moment is shown to arise from a non-Debye component of water polarization created by nanoscale packing defects on the protein surface. Accordingly, the protein electrostatic field exerts a torque on the induced dipole, locally impeding the nucleation of ice at the protein–water interface. We evaluate the solvent orientation steering (SOS) as the reversible work needed to align the induced dipoles with the Debye electrostatic field and computed the SOS for the variable interface of a folding protein. The minimization of the SOS is shown to drive protein folding as evidenced by the entrainment of the total free energy by the SOS energy along trajectories that approach a Debye limit state where no torque arises. This result suggests that the minimization of anomalous water polarization at the interface promotes the sealing of packing defects, thereby maintaining structural integrity and committing the protein chain to fold.
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática; Argentina. Collegium Basilea; Suiza
Materia
Protein Structure
Biophysics
Soft Matter Physics
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:11336/12174

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network_name_str CONICET Digital (CONICET)
spelling Water promotes the sealing of nanoscale packing defects in folding proteinsFernandez, ArielProtein StructureBiophysicsSoft Matter PhysicsDehydronhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1A net dipole moment is shown to arise from a non-Debye component of water polarization created by nanoscale packing defects on the protein surface. Accordingly, the protein electrostatic field exerts a torque on the induced dipole, locally impeding the nucleation of ice at the protein–water interface. We evaluate the solvent orientation steering (SOS) as the reversible work needed to align the induced dipoles with the Debye electrostatic field and computed the SOS for the variable interface of a folding protein. The minimization of the SOS is shown to drive protein folding as evidenced by the entrainment of the total free energy by the SOS energy along trajectories that approach a Debye limit state where no torque arises. This result suggests that the minimization of anomalous water polarization at the interface promotes the sealing of packing defects, thereby maintaining structural integrity and committing the protein chain to fold.Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática; Argentina. Collegium Basilea; SuizaIop Publishing2014-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/12174Fernandez, Ariel; Water promotes the sealing of nanoscale packing defects in folding proteins; Iop Publishing; Journal Of Physics: Condensed Matter; 26; 20; 5-2014; 1-7; 2021010953-8984enginfo:eu-repo/semantics/altIdentifier/url/http://iopscience.iop.org/0953-8984/26/20/202101/info:eu-repo/semantics/altIdentifier/doi/10.1088/0953-8984/26/20/202101info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:55:20Zoai:ri.conicet.gov.ar:11336/12174instacron: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 09:55:20.627CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Water promotes the sealing of nanoscale packing defects in folding proteins
title Water promotes the sealing of nanoscale packing defects in folding proteins
spellingShingle Water promotes the sealing of nanoscale packing defects in folding proteins
Fernandez, Ariel
Protein Structure
Biophysics
Soft Matter Physics
Dehydron
title_short Water promotes the sealing of nanoscale packing defects in folding proteins
title_full Water promotes the sealing of nanoscale packing defects in folding proteins
title_fullStr Water promotes the sealing of nanoscale packing defects in folding proteins
title_full_unstemmed Water promotes the sealing of nanoscale packing defects in folding proteins
title_sort Water promotes the sealing of nanoscale packing defects in folding proteins
dc.creator.none.fl_str_mv Fernandez, Ariel
author Fernandez, Ariel
author_facet Fernandez, Ariel
author_role author
dc.subject.none.fl_str_mv Protein Structure
Biophysics
Soft Matter Physics
Dehydron
topic Protein Structure
Biophysics
Soft Matter Physics
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 A net dipole moment is shown to arise from a non-Debye component of water polarization created by nanoscale packing defects on the protein surface. Accordingly, the protein electrostatic field exerts a torque on the induced dipole, locally impeding the nucleation of ice at the protein–water interface. We evaluate the solvent orientation steering (SOS) as the reversible work needed to align the induced dipoles with the Debye electrostatic field and computed the SOS for the variable interface of a folding protein. The minimization of the SOS is shown to drive protein folding as evidenced by the entrainment of the total free energy by the SOS energy along trajectories that approach a Debye limit state where no torque arises. This result suggests that the minimization of anomalous water polarization at the interface promotes the sealing of packing defects, thereby maintaining structural integrity and committing the protein chain to fold.
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática; Argentina. Collegium Basilea; Suiza
description A net dipole moment is shown to arise from a non-Debye component of water polarization created by nanoscale packing defects on the protein surface. Accordingly, the protein electrostatic field exerts a torque on the induced dipole, locally impeding the nucleation of ice at the protein–water interface. We evaluate the solvent orientation steering (SOS) as the reversible work needed to align the induced dipoles with the Debye electrostatic field and computed the SOS for the variable interface of a folding protein. The minimization of the SOS is shown to drive protein folding as evidenced by the entrainment of the total free energy by the SOS energy along trajectories that approach a Debye limit state where no torque arises. This result suggests that the minimization of anomalous water polarization at the interface promotes the sealing of packing defects, thereby maintaining structural integrity and committing the protein chain to fold.
publishDate 2014
dc.date.none.fl_str_mv 2014-05
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/11336/12174
Fernandez, Ariel; Water promotes the sealing of nanoscale packing defects in folding proteins; Iop Publishing; Journal Of Physics: Condensed Matter; 26; 20; 5-2014; 1-7; 202101
0953-8984
url http://hdl.handle.net/11336/12174
identifier_str_mv Fernandez, Ariel; Water promotes the sealing of nanoscale packing defects in folding proteins; Iop Publishing; Journal Of Physics: Condensed Matter; 26; 20; 5-2014; 1-7; 202101
0953-8984
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://iopscience.iop.org/0953-8984/26/20/202101/
info:eu-repo/semantics/altIdentifier/doi/10.1088/0953-8984/26/20/202101
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 Iop Publishing
publisher.none.fl_str_mv Iop Publishing
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