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dc.contributor.author
Fernandez, Ariel
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dc.date.available
2017-06-08T14:48:32Z
dc.date.issued
2012-04
dc.identifier.citation
Fernandez, Ariel; Epistructural thermodynamics of soluble proteins; American Institute Of Physics; Journal Of Chemical Physics; 136; 9; 4-2012; 1-4; 91101
dc.identifier.issn
0021-9606
dc.identifier.uri
http://hdl.handle.net/11336/17756
dc.description.abstract
The epistructural tension of a soluble protein is defined as the reversible work per unit area required to span the interfacial solvent envelope of the protein structure. It includes an entropic penalty term to account for losses in hydrogen-bonding coordination of interfacial water and is determined by a scalar field that indicates the expected coordination of a test water molecule at any given spatial location. An exhaustive analysis of structure-reported monomeric proteins reveals that disulfide bridges required to maintain structural integrity provide the thermodynamic counterbalance to the epistructural tension, yielding a tight linear correlation. Accordingly, deviations from the balance law correlate with the thermal denaturation free energies of proteins under reducing conditions. The picomolar-affinity toxin HsTX1 has the highest epistructural tension, while the metastable cellular form of the human prion protein PrPC represents the least tension-balanced protein.
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.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Protein
dc.subject
Disulfide Bond
dc.subject
Interfacial Tension
dc.subject.classification
Otras Ciencias Físicas
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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
Epistructural thermodynamics of soluble proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-05-15T17:57:17Z
dc.journal.volume
136
dc.journal.number
9
dc.journal.pagination
1-4; 91101
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Nueva York
dc.description.fil
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Saavedra 15. Instituto Argentino de Matemática Alberto Calderon; Argentina
dc.journal.title
Journal Of Chemical Physics
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1063/1.3691890
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://aip.scitation.org/doi/10.1063/1.3691890
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