Eduardo Perozo
The University of Chicago
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Primary Section: 23, Physiology and Pharmacology Secondary Section: 29, Biophysics and Computational Biology Membership Type:
Member
(elected 2023)
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Biosketch
Eduardo Perozo is Professor in the Department of Biochemistry and Molecular Biology at the University of Chicago. He obtained a Licenciado Degree in Biology at the Universidad Central de Venezuela (UCV) and his Ph.D in Physiology at the University of California, Los Angeles. He was a postdoctoral fellow in membrane biophysics at the Jules Stein Eye Institute and Dept. of Chemistry and Biochemistry, UCLA. After a short tenure as Assistant Investigator at the Instituto Venezolano de Investigaciones Científicas (IVIC), Perozo joined the Department of Physiology and Biological Physics at the University of Virginia, as Assistant Professor. In 2006 he joined the faculty of the Department of Biochemistry and Molecular Biology and became a member of the Institute for Biophysical Dynamics and the Neuroscience Institute. He currently serves as Director of the Center for Mechanical Excitability. He was elected as a Fellow of the Biophysical Society in 2015 and in 2019 received the KS Cole Award for contributions to our understanding of ion channel structure and dynamics. In 2023 he was inducted to the Academia de Ciencias de America Latina (ACAL).
Research Interests
Perozo aims to understand the mechanism of ion channel gating at the molecular level and the processes that define energy transduction in membrane proteins. He is particularly focused on the elucidation of structure-function relations associated to two fundamental energy transduction processes, voltage dependence and mechanotransduction in sensory systems. The Perozo lab follows a multidisciplinary approach that takes advantage of a variety of experimental techniques: membrane protein biochemistry, an electrophysiological handle on function, spectroscopic approaches to follow local and global dynamics, the capacity to generate conformationally specific high-resolution structures by cryo-EM, and powerful computational approaches to define and evaluate the energy landscape of membrane proteins.
