Ann McDermott is the Esther Breslow Professor of Biological Chemistry at Columbia University. She holds a B.Sc. in Chemistry from Harvey Mudd College, and a Ph.D. in Chemistry from U.C. Berkeley, where she worked with Kenneth Sauer and Melvin Klein; subsequently she had postgraduate training at MIT with Dr. Robert Griffin.
Her research concerns the remarkable ability of naturally occurring proteins to catalyze chemical reactions, focusing specifically on the inherent flexibility of enzymes and the coordination of chemistry to conformational exchange, using magnetic resonance methods. Her group carries out assignment and analysis of high-resolution MAS-based NMR spectra of proteins, including intrinsic membrane proteins in native lipid bilayers, microcrystalline proteins, large native assemblies like viral coats, and fibrillar or amyloid proteins.
She is the recipient of the Pure Award in Chemistry (1996) and the Eastern Analytic Symposium Award for Achievement in Magnetic Resonance (2005), and she is an elected member of both the American Academy of Arts and Sciences, and the National Academy of Sciences. At Columbia University she recently served as Associate Vice President for Academic Advising and Science Initiatives in the Arts and Sciences.
My research is focused on connecting structural and functional states of KcsA, a model bacterial potassium channel, as it undergoes activation, potassium conduction, and subsequent inactivation. I am particularly interested in the C-type inactivation process, in which the channel slowly inactivates spontaneously after activation. By combining solid-state NMR with other biophysical methods, including electrophysiology and site-directed mutagenesis, my work elucidates the strong allosteric coupling between the activation gate and the potassium selectivity filter and connects this allostery to the functional role of the channel in controlling potassium ion permeation.
I am focused on determining the structure and chemical kinetics of macromolecular systems, including of segments previously described as disordered. Currently, I use high-resolution solid-state NMR, and Dynamic Nuclear Polarization (DNP) enhanced experiments to study a full-length protein with a prion-like domain in a condensed/ aggregated state. This class of proteins is involved in numerous protein misfolding disease and has a complex structural landscape. I have two other parallel projects where I am building tools to further studies of systems with intermediate time-scale kinetics. (1) I have constructed and am testing a microsecond time-scale freeze quenching apparatus for solid-state NMR samples. (2) Collaboratively with other members of the McDermott Group, we are designing improved solid-state NMR pulse sequences for characterizing protein dynamics with spin-locking fields.
My research focuses on protein structure and dynamics in the solid state utilizing solid state nuclear magnetic resonance spectroscopy.
My research focuses on the effect of lipids on the structure and dynamic of membrane proteins.
My research interests are primarily focused on the structure and dynamics of cytoskeletal assemblies, and my current project uses solid state NMR to explore the bacterial cytoskeleton. I am also interested in whole cell DNP and in using solid state NMR to address questions of biological importance. Outside the lab I am an unknowable cryptid who haunts coffee shops and hockey rinks.
2016-present Chemistry Ph.D; 2012-2016 Tsinghua University B.S.
I am interested in Dynamic Nuclear Polarization, and love learning NMR!
I like NMR too.