Artículo
Epistructural thermodynamics of soluble proteins
Fecha de publicación:
04/2012
Editorial:
American Institute Of Physics
Revista:
Journal Of Chemical Physics
ISSN:
0021-9606
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Palabras clave:
Protein
,
Disulfide Bond
,
Interfacial Tension
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Articulos(IAM)
Articulos de INST.ARG.DE MATEMATICAS "ALBERTO CALDERON"
Articulos de INST.ARG.DE MATEMATICAS "ALBERTO CALDERON"
Citación
Fernandez, Ariel; Epistructural thermodynamics of soluble proteins; American Institute Of Physics; Journal Of Chemical Physics; 136; 9; 4-2012; 1-4; 91101
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