Events & Seminars > Event Details


4:00 pm
Room 304, Chemistry Building

NMR of conditional peripheral membrane domains


Professor Tatyana Igumenova
Texas A&M University

Hosted by: Professor Dave Cafiso

Conditional membrane proteins associate with membranes in response to binding specific ligands. We report the application of NMR techniques to gain insight into the structure, dynamics, and protein-membrane interactions of two fundamentally different conditional membrane modules, C1 and C2 domains from Protein Kinase C. Using NMR relaxation dispersion techniques, paramagnetic relaxation enhancement experiments, and NMR-detected ligand binding studies, we demonstrate the role of conformational plasticity and initial membrane pre-association in modulating the affinity of the C1 domain to its natural cofactor, diacylglycerol. We show that the C2 domain employs a drastically different mechanism of membrane insertion that involves (i) modulation of its electrostatic potential by divalent metal ions, and (ii) specific metal-lipid interactions.


Professor Igumenova received her Ph.D. degree in Physical Chemistry from Columbia University, working under the guidance of Dr. Ann McDermott on the development and application of multidimensional solid-state NMR methods for protein structure determination.  As a postdoctoral trainee in the laboratory of Dr. A. Joshua Wand at UPenn and later in Dr. Arthur G. Palmer’s laboratory at Columbia University’s Medical School, she worked on both application and development of NMR relaxation methods to investigate functionally relevant motions in proteins.  In 2008, she joined the Department of Biochemistry and Biophysics at Texas A&M University as an Assistant Professor.  The major research focus of her laboratory is the investigation of structural and dynamical basis of Protein Kinase C regulation.