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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/12174
Ver los metadatos del registro completo
id |
CONICETDig_f25c0e269436d46b79f54cc0fbf0fd99 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/12174 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
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 |
_version_ |
1844613669450678272 |
score |
13.070432 |