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David D. Thomas
Professor, BMBB

Ph.D., Stanford University (H. McConnell) - Biophysics

Contact Information:

Office: 5-124 NHH

Telephone: 612-625-0957
Fax: 612-624-0632
E-mail: ddt@umn.edu

Laboratory: 5-290 NHH
Telephone: 612-626-3322

Lab Web Site
BMBB Home > Faculty
David D. Thomas [ Back ]

 

David D. Thomas

 

Research Interests
 
Molecular dynamics of energy transduction in muscle, using site-directed spectroscopic probes

 

Research Description

Our goal is to understand the fundamental molecular motions and interactions that are responsible for cellular movement, and to determine the molecular bases of muscle disorders. We approach this multidisciplinary problem with a wide range of techniques -- physiology, enzyme kinetics, molecular genetics, peptide synthesis, computer simulation -- but our forte is site-directed spectroscopic probes. After attaching site-directed probes (spin labels, fluorescent dyes, phosphorescent dyes, or isotopes) to selected muscle proteins in solution or in cells, we perform magnetic resonance or optical spectroscopy to directly detect the motions of the force-generating proteins, actin and myosin, or the membrane ion pumps and channels responsible for muscle excitation and relaxation.


Recent Publications

 

Lowe, D.A., B.O. Williams, D.D. Thomas and R.W. Grange. 2006. Molecular and cellular contractile dysfunction of dystrophic muscle from young mice. Muscle Nerve 34: 92-100.

Traaseth, N.J., D.D. Thomas and G. Veglia. 2006. Effects of Ser16 phosphorylation on the allosteric transitions of phospholamban/Ca(2+)-ATPase complex. J Mol Biol, in press.

Karim, C.B., Z. Zhang, E.C. Howard, K.D. Torgersen and D.D. Thomas. 2006. Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA. J Mol Biol, 358: 1032-40.

Buffy, J.J., B.A. Buck-Koehntop, F. Porcelli, N.J. Traaseth, D.D. Thomas and G. Veglia. 2006. Defining the intramembrane binding mechanism of sarcolipin to calcium ATPase using solution NMR spectroscopy. J Mol Biol, 358: 420-9.

Traverse J.H., Y. E. Nesmelov, M. Crampton, P. Lindstrom, D. D. Thomas and R. J. Bache. 2006. Measurement of myocardial free radical production during exercise using EPR spectrscopy. Am J Physiol Heart Circ Physiol, e-published.

Zhang, J., B. J. Wallar, C. V. Popescu, D. B. Renner, D. D. Thomas, and J. D. Lipscomb. 2006. Methane monooxygenase hydroxylase and B component interactions. Biochemistry, 45: 2913-26. 2006.

Nesmelov, Y. E. and D. D. Thomas. Multibore sample cell increases EPR sensitivity for aqueous samples. 2005. J of Magn Reson, 178: 318-24.

Prochniewicz, E., N. Janson, D. D. Thomas, and E. M. De La Cruz. 2005. Cofilin increases the torsional flexibility and dynamics of actin filaments. J Molec Biol, 353, 990-1000.

Korman, V. L., S. E. B. Anderson, E. Prochniewicz, M. A. Titus and D. D. Thomas. 2005. Structural dynamics of the actin-myosin interface by site-directed spectroscopy. J Molec Biol, 356: 1107-17.

Balog, E. M., L. E. Norton, D. D. Thomas and B. R. Fruen. 2005. Role of calmodulin methionine residues in mediating the productive association with cardiac ryanodine receptors. Am J Physiol Heart Circ Physiol, 290: H794-9.

Prochniewicz, E., D. D. Thomas, and L. V. Thompson. 2005. Age-related decline in actomyosin function. J Gerontol A Biol Sci, 60A (4): 425-431.

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The University of Minnesota is an equal opportunity educator and employer. Last modified: April 16, 2009