The Faculty
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Eduardo Perozo
Professor, Biochemistry & Molecular Biokogy, Institute for Biophysical Dynamics; Pritzker Fellow, The University of Chicago
Affiliation: Biochemistry & Molecular Biology, Institute for Biophysical Dynamics
Emaileperozo@uchicago.edu
Websitehttps://bcmb.uchicago.edu/program/faculty/eduardo-perozo
Focus
Ion channels, membrane transport, membrane protein dynamics, energy transduction mechanisms, voltage dependent processes. Over-expression of membrane proteins
Education
Universidad Central de Venezuela, Caracas, Facultad de Ciencias, Licenciado , 1980‑1985, Biology
University of California, Los Angeles, Ph.D., 1987-1990, Physiology
University of California, Los Angeles, Post Doc, 1991-1993, Membrane Biophysics
Biography
May‑Aug 1986 Grass Fellow. Grass Foundation, Marine Biological Laboratory. Woods Hole, Massachusetts.
1987 Chancellor's Fellow. University of California, Los Angeles
1989 Kugel Foundation Fellow, Department of Physiology, University of California, Los Angeles
1990 John Field Award, Department of Physiology, University of California, Los Angeles, CA.
1991- 1993 PEW Charitable Trust Latin American Fellowship, University of California, Los Angeles, CA.
1994 PPI Program Fellow, Level II. Consejo Nacional de Investigaciones Cientificas y Tecnologicas (CONICIT) Caracas, Venezuela.
1998-2000 McKnight Fellow, University of Virginia.
2000 SOBLA Prize, Latin-American Society of Biophysicists. Alicante, Spain.
2004 Kuffler/MBL Fellowships. Marine Biological Laboratory, Woods Hole, MA.
2006-present Pritzker Fellow, The University of Chicago
Research Summary
Most membrane proteins have moving parts that help execute their specific function, often in response to an external stimulus. Our research aims to understand the molecular mechanisms underlying the transduction of different forms of energy into protein motion; in particular the different molecular mechanisms of ion channel gating. We are equally interested in protein structure as in protein dynamics, for it is the dynamic behavior of a molecule what links structure to function.
Therefore, we rely on spectroscopic methods, and in particular reporter group techniques (EPR, Fluorescence), to study channels and other membrane proteins embedded in a fluid lipid bilayer. Static structural analyses are pursued by X-ray crystallography. These structural techniques are all interpreted in the context of high-resolution functional methods (single channel, macroscopic and gating current electro-physiological measurements). Using these strategies, we aim to answer the following long-term questions:
1- What is the structural pathway followed in the transition from the closed to the open conformation in K+ channels, and what is the nature of this conformational wave?
2- What is the influence of the selectivity filter on channel gating?
3- What is the native structure of voltage-dependent channels and how is transmembrane voltage sensed?
4- How do voltage sensor and gate couple to open the channel?
5- What is the molecular basis of mechanosensitivity in prokaryotic channels? How do membrane bilayer deformations are transduced into large protein rearrangements leading to channel opening?
