0000000000582742

AUTHOR

Carmina Verdiá-báguena

showing 2 related works from this author

Energy transduction and signal averaging of fluctuating electric fields by a single protein ion channel

2016

[EN] We demonstrate the electrical rectification and signal averaging of fluctuating signals using a biological nanostructure in aqueous solution: a single protein ion channel inserted in the lipid bilayer characteristic of cell membranes. The conversion of oscillating, zero time-average potentials into directional currents permits charging of a load capacitor to significant steady-state voltages within a few minutes in the case of the outer membrane porin F (OmpF) protein, a bacterial channel of Escherichia coli. The experiments and simulations show signal averaging effects at a more fundamental level than the traditional cell and tissue scales, which are characterized by ensembles of many…

0301 basic medicineLipid BilayersPorinsGeneral Physics and AstronomyNanotechnology02 engineering and technologyMolecular physicsIon Channelslaw.invention03 medical and health scienceslawElectric fieldEscherichia coliPhysical and Theoretical ChemistryLipid bilayerIon channelbiologyChemistryCell MembraneElectric Conductivity021001 nanoscience & nanotechnologybiology.organism_classificationCapacitor030104 developmental biologyMembraneFISICA APLICADASignal averagingNanodiodes0210 nano-technologyBacterial Outer Membrane ProteinsVoltagePhysical Chemistry Chemical Physics
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Entropy–enthalpy compensation at the single protein level: pH sensing in the bacterial channel OmpF

2014

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. We wish to acknowledge the support from the Span…

Models Molecularentropy-enthalpy compensationChemistryLigandEntropyEnthalpyBinding energyElectric ConductivitypH sensingPorinsConductanceThermodynamicsHydrogen-Ion ConcentrationThermal conductionbinding energyPotassium ChlorideSolventModels ChemicalComputer SimulationGeneral Materials Sciencesense organsBinding siteskin and connective tissue diseasesentropyEntropy (order and disorder)
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