Tatyana Igumenova
Assistant Professor of Biochemistry and BiophysicsPhone: (979) 845-6312 Email: tigumenova@tamu.edu Ph.D. Columbia University, 2003 Postdoc. University of Pennsylvania, 2003-2005 Postdoc. Columbia University, 2005-2007 Igumenova Lab Website Joined Texas A&M Faculty 2008 |
Protein Dynamics and NMR |
| The importance of Nuclear Magnetic Resonance (NMR) methods in structural biology is illustrated by the rapidly growing number of three-dimensional NMR structures in the Protein Data Bank. While well-folded soluble proteins make up the majority of these structures, membrane-associated, partially folded, aggregated, and heterogeneous protein systems are also amenable to solution and solid-state NMR studies. In addition to structural data, NMR is able to provide site-resolved information on dynamical processes that occur on the timescale from seconds to picoseconds. In particular, NMR relaxation techniques for the characterization of dynamical processes on the microsecond-to-millisecond timescale provide a powerful tool for the investigation of protein folding, catalysis, ligand binding, and allosteric phenomena. Our laboratory uses advanced solid-state and solution NMR techniques to explore the structure and dynamics of membrane-associated proteins and to investigate the role of conformational dynamics in enzymatic catalysis and protein-protein recognition. Protein systems of interest include (i) lipid-binding domains of Protein Kinase C (PKC) isoenzymes, whose role in cell proliferation, apoptosis, and cancer progression has made them an important therapeutic target, and (ii) Rab GTPases, which serve as primary regulators of intracellular vesicle trafficking by cycling between their GDP-bound (inactive) and GTP-bound (active) states. |
Recent Publications |
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