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dc.contributor.author
Fernandez, Ariel
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dc.date.available
2016-01-06T14:22:41Z
dc.date.issued
2013-08
dc.identifier.citation
Fernandez, Ariel; The principle of minimal episteric distortion of the water matrix and its role in protein folding; American Institute Of Physics; Journal Of Chemical Physics; 139; 8-2013; 85101-85101
dc.identifier.issn
0021-9606
dc.identifier.uri
http://hdl.handle.net/11336/3365
dc.description.abstract
A significant episteric (around a solid) distortion of the hydrogen-bond structure of water is promoted by solutes with nanoscale surface detail and physico-chemical complexity, such as soluble natural proteins. These structural distortions defy analysis because the discrete nature of the solvent at the interface is not upheld by the continuous laws of electrostatics. This work derives and validates an electrostatic equation that governs the episteric distortions of the hydrogen-bond matrix. The equation correlates distortions from bulk-like structural patterns with anomalous polarization components that do not align with the electrostatic field of the solute. The result implies that the interfacial energy stored in the orthogonal polarization correlates with the distortion of the water hydrogen-bond network. The result is validated vis-à-vis experimental data on protein interfacial thermodynamics and is interpreted in terms of the interaction energy between the electrostatic field of the solute and the dipole moment induced by the anomalous polarization of interfacial water.Finally, we consider solutes capable of changing their interface through conformational transitions and introduce a principle of minimal episteric distortion (MED) of the water matrix. We assess the importance of the MED principle in the context of protein folding, concluding that the native fold may be identified topologically with the conformation that minimizes the interfacial tension or disruption of the water matrix.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Institute Of Physics
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights
Atribución-NoComercial-CompartirIgual 2.5 Argentina (CC BY-NC-SA 2.5 AR)
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Episteric Tension
dc.subject
Protein Folding
dc.subject
Dehydron
dc.subject
Interfacial Tension
dc.subject.classification
Física Atómica, Molecular y Química
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dc.subject.classification
Ciencias Físicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
The principle of minimal episteric distortion of the water matrix and its role in protein folding
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-30 10:35:44.97925-03
dc.journal.volume
139
dc.journal.pagination
85101-85101
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
New York
dc.description.fil
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemáticas; Argentina
dc.journal.title
Journal Of Chemical Physics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://scitation.aip.org/content/aip/journal/jcp/139/8/10.1063/1.4818874
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/10.1063/1.4818874
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1063/1.4818874
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