Atomistic Resolution Dances of Membrane Proteins by NMR

Dr. Ayyalusamy Ramamoorthy, Professor
Biophysics and Department of Chemistry, University of Michigan
Date: September 25, 2015
Place: Chem-Sci Room 101
Time: 3:00 pm


Membrane proteins are an exciting class of biomacromolecules and play important roles in a variety of biological processes that are directly linked to major diseases including cancer, aging-related diseases, and infectious diseases. A complete understanding of their function can only be accomplished using high-resolution structures and dynamics. In spite of recent developments in structural biology, membrane proteins continue to pose tremendous challenges to most biophysical techniques. A major area of research in my group is focused on the development of NMR techniques to study the dynamic structures of membrane bound proteins such as cytochrome b5, cytochrome P450 and cytochrome P450-reductase. In my talk, I will present strategies to study the structure and dynamics of these challenging systems and also on the electron transfer mechanism that enables the enzymatic function of P450. Atomic-level resolution NMR structures of amyloidogenic proteins revealing the misfolding pathway and early intermediates that play key roles in amyloid toxicity will also be presented.
J. Biol. Chem. (2015) 290:12705-18; 290: 4843-55; 288:22080-95.
Chem. Soc. Rev. (2014) 43:6692-6700; J. Phys. Chem. Lett. (2014) 5:1864.


Dr. Ayyalusamy Ramamoorthy is Professor of Biophysics and Chemistry at University of Michigan, where he has been since 1996. He has applied NMR spectroscopy and other biophysical techniques to investigate high-resolution structure, dynamics, and functional properties of membrane proteins, amyloid proteins/peptides, and antimicrobial peptides. He has published more than 250 peer-reviewed papers in leading high impact journals like Science, PNAS, JACS, J. Biol. Chem., and Angew. Chem. Eng. Intl., written several review articles, edited 2 books on NMR spectroscopy, brought out several special issues as a guest editor, and organized several conferences related to NMR spectroscopy. He is a member of editorial boards of J. Biol. Chem., Plos One, Scientific Reports, Peer J, Biochimica Biophysica Acta, Journal of Magnetic Resonance, Chemistry and Physics of Lipids, Solid State Nuclear Magnetic Resonance Spectroscopy, and Magnetic Resonance in Chemistry. He has been a PI or co-PI on several NIH (and other) sponsored projects.
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