Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpF
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Other documents of the author: Alcaraz, Antonio; Queralt-Martín, María; Verdiá Báguena, Carmen; Aguilella, Vicente; Mafe, Salvador
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comunitat-uji-handle3:10234/6973
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http://dx.doi.org/10.1039/c4nr03811h |
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Title
Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpFAuthor (s)
Date
2014Publisher
The Royal Society of ChemistryBibliographic citation
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.Type
info:eu-repo/semantics/articlePublisher version
http://pubs.rsc.org/en/content/articlehtml/2014/nr/c4nr03811hVersion
info:eu-repo/semantics/publishedVersionSubject
Abstract
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 24Rights
© The Royal Society of Chemistry 2014
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