Evgenii Kovrigin, Ph.D.
Assistant Professor
Dr. Kovrigin obtained his doctoral degree in Chemistry from the Engelhardt Institute of Molecular Biology (Moscow, Russia) in 1999. His doctoral studies of protein thermodynamics in mixed solvents (at the Institute of Protein Research, Pushchino, Russia) brought him "Microcal Young Scientist Award 1999" presented to him at 2nd International Conference on Applications of Biocalorimetry 1999 (Halle/Saale., Germany). Dr. Kovrigin's post-doctoral work at UT Southwestern, Dallas and Yale University, New Haven was focused on determination of tertiary structure and dynamic behavior of proteins by means of NMR spectroscopy. Dr. Kovrigin joined the faculty of the Medical College of Wisconsin in 2006.
Contact Information
ekovrig@mcw.edu
Phone: (414) 955-5885
Fax: (414) 456-6510
Research Interests
Nuclear Magnetic Resonance (NMR) spectroscopy is a unique multi-faceted tool for biochemical and biophysical studies. This rapidly developing technique allows probing molecular structure and dynamics as well as protein-ligand interactions, determination of kinetic and thermodynamic parameters of macromolecules and complexes all with atomic resolution.
My laboratory uses NMR spectroscopy to address important biological problems. We complement power of NMR experiments with other biophysical approaches such as microcalorimetry, X-ray diffraction, fluorescent and CD-spectroscopy as well as computational techniques.
One of the major projects in the lab is focused on small Ras-like GTPases and their involvement in signaling and cancer development. Ras GTPase is a prototypical example of Ras superfamily proteins responsible for signal transduction in a multitude of cellular processes including growth, development, proliferation and apoptosis. Ras-like GTPases display puzzling capacity to interact with a large number of downstream effectors all responsible for different signaling pathways. The way molecular features of Ras GTPases determine its signaling activity is a focus of our studies. We anticipate to contribute to understanding of cellular signaling as well as to specifically address cancer-related properties and interactions of Ras GTPase isoforms.
Another direction in the laboratory is the development of methodology for studies of protein-ligand and protein-protein interactions via NMR line shape analysis. LineShapeKin software package has been developed to assist analysis of the line shapes of the experimental HSQC spectra and extract constants of association/dissociation kinetics from HSQC titrations. This software has been presented on a poster at 49th Experimental NMR Conference and is freely distributed to all academic users from http://lineshapekin.net/.
Selected Publications
"The mechanism of rate-limiting motions in enzyme function." Watt, ED, Shimada, H, Kovrigin, EL, and Loria, JP, PNAS, 104, 11981-11986 (2007) This publication was presented in Research Highlights. Nat. Struct. Mol. Biol., 14, 688 (2007).
"Characterization of the transition state of functional enzyme dynamics."Kovrigin EL and Loria JP, J. Am. Chem. Soc., 128:7724-7725 (2006)
"Faithful Estimation of Dynamics Parameters from CPMG Relaxation Dispersion Measurements" Kovrigin EL, Kempf JG, Grey MJ, Loria JP, J. Mag. Res., 180:93-104 (2006)
"Enzyme dynamics along the reaction coordinate: Critical role of a conserved residue" Kovrigin EL, Loria JP, Biochemistry 45, 2636-2647 (2006)
"NMR studies of Escherichia coli acyl carrier protein: Dynamic and structural differences of the apo- and holo-forms" Kim Y, Kovrigin EL, Eletr Z, Biochem. Biophys. Res. Commun. 341: 776-783 (2006)
"Temperature dependence of the backbone dynamics of Ribonuclease A in the ground state and bound to the inhibitor, 5'-phosphothymidine (3'-5')-pyrophosphate adenosine 3'-phosphate." Kovrigin EL, Cole R, Loria JP, Biochemistry 42: 5279-5291 (2003)
"Three-dimensional structure of the complexin/SNARE complex." Chen X, Tomchick DR, Kovrigin E, Arac D, Machius M, Sudhof TC, Rizo J. Neuron 33: 397-409 (2002)
"On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions." Kovrigin E.L., Potekhin S.A. Biophysical Chemistry 83: 45-59 (2000)
"Effect of kinetic factors on heat denaturation and renaturation of biopolymers" Potekhin S.A., Kovrigin E.L., Biophysics 43: 198-207 (1998)
"Folding under inequilibrium conditions as a possible reason for partial irreversibilty of heat-denatured proteins: computer simulation study." Potekhin S.A., Kovrigin E.L. Biophysical Chemistry 73: 241-248 (1998)
"Preferential solvation changes upon lysozyme heat denaturation in mixed solvents" Kovrigin E.L., Potekhin S.A., Biochemistry 36: 9195-9199 (1997)
"Microcalorimetric study of the effect of dimethylsulphoxide on the heat denaturing of lysozyme" Kovrigin Ye.L., Potekhin S.A., Biophysics 41: 1219-1224 (1996)
"Enthalpy of stabilization of the structure of hen's egg lysozyme in aqueous solutions of dimethyl sulphoxide" Kovrigin Ye.L., Kirkitadze M.D., Potekhin S.A., Biophysics 41: 547-551 (1996)