Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpF
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Scholar |
Otros documentos de la autoría: Alcaraz, Antonio; Queralt-Martín, María; Verdiá Báguena, Carmen; Aguilella, Vicente; Mafe, Salvador
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http://dx.doi.org/10.1039/c4nr03811h |
Metadatos
Título
Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpFAutoría
Fecha de publicación
2014Editor
The Royal Society of ChemistryCita bibliográfica
ALCARAZ, Antonio, et al. Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpF. Nanoscale, 2014, vol. 6, no 24, p. 15210-15215.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.rsc.org/en/content/articlehtml/2014/nr/c4nr03811hVersión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
The pH sensing mechanism of the OmpF channel operates via ligand modification: increasing acidity induces the replacement of cations with protons in critical binding sites decreasing the channel conductance. Aside ... [+]
The pH sensing mechanism of the OmpF channel operates via ligand modification: increasing acidity induces the replacement of cations with protons in critical binding sites decreasing the channel conductance. Aside from the change in enthalpy associated with the binding, there is also a change in the microscopic arrangements of ligands, receptors and the surrounding solvent. We show that the pH-modulation of the single channel conduction involves small free energy changes because large enthalpic and entropic contributions change in opposite ways, demonstrating an approximate enthalpy–entropy compensation for different salts and concentrations. [-]
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Nanoscale, 2014, vol. 6, no 24Derechos de acceso
© The Royal Society of Chemistry 2014
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