Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Bezanilla, Francisco
Location The University of Chicago
Primary Field Physiology and Pharmacology
Secondary Field Biophysics and Computational Biology
 Election Citation
An investigator of extraordinary virtuosity, Bezanilla has contributed to our understanding of the voltage-driven changes that underlie ion channel gating. He is a pathfinder in use of fluorescent labeling techniques for studying dynamic rearrangement in channel proteins, and codiscoverer of gating current in sodium channels.
 Research Interests
Since the beginning of my scientific career I have been interested in voltage dependent phenomena in cell Physiology. These include the description of the biophysical events of channel function that generate the nerve impulse and the adaptation of these channels to maintain the function of the nervous system in environment where organisms live for. My initial studies were directed to the detailed understanding of the conductance changes during the action potential, followed by studies of voltage gated conductances and the first recordings of the movement of charges (gating currents) responsible for the voltage detection in the nerve membrane. The description of gating currents, macroscopic and single channel ionic currents in voltage-gated channels allowed us to model the voltage sensor as a black box. Only after molecular cloning became available we were able to identify the elements inside the black box and pinpoint the amino acids responsible for the charge movement. Presently, we are monitoring the correlation of the electrical events with structural changes in the channel molecule using real time fluorescence spectroscopy including single molecule fluorescence, lifetimes, quenching and fluorescence resonance energy transfer from probes attached to strategic sites in the molecule of interest while being functional in the membrane. My present interest is the understanding of the dynamics of the molecular correlates of the function in voltage-modulated membrane transport proteins.

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