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faculty profile |
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Research Description:
The Yengo group studies the structure and function properties of molecular motor proteins. These proteins are capable of converting chemical energy into mechanical work to drive the processes of muscle contraction, intracellular transport, and cell division. The Yengo group is examining the structural mechanism of energy transduction in myosin motor proteins using spectroscopic and biophysical methods. In addition, studies of uncharacterized non-muscle myosin proteins that function in vision and hearing are in progress to understand their enzymatic, structural and regulatory properties. The regulation of smooth muscle myosin contraction and its role in disease conditions is also under investigation. In collaboration with Ken Gonsolves in the Department of Chemistry, the biophysical properties of potential drug delivery vehicles for Muscular Dystrophy are being characterized. |
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Recent Publications:
M. Sun, J.L. Oakes, S.K. Ananthanarayanan, K.H. Hawley, R.Y. Tsien, S.R. Adams, C.M. Yengo (2006). Dynamics of the upper 50 kDa domain of myosin V examined with fluorescence resonance energy transfer. Journal of Biological Chemistry, 281:5711-5717.
J. Menetrey, A. Bahloul, A.L. Wells, C.M. Yengo, C.A. Morris, H.L. Sweeney, A. Houdusse (2005). The structure of the myosin VI motor reveals the mechanism of directionality reversal. Nature, 435:779-785.
K.N. Wallace, A.C. Dolan, C. Seiler, E.M. Smith, S. Yusuff, L. Chaille-Arnold, B. Judson, R. Sierk, C. Yengo, H.L. Sweeney, M. Pack (2005). Mutation of smooth muscle myosin causes invasion and cystic expansion of the zebrafish intestine. Developmental Cell, 8:717-726.
B. Ramamurthy, C.M. Yengo, A.F. Straight, T.J. Mitchison, H.L. Sweeney (2004). Kinetic mechanism of blebbistatin inhibition of nonmuscle myosin IIB. Biochemistry, 43:14832-14839.
C.M. Yengo, H.L. Sweeney (2004). Functional role of loop 2 in myosin V. Biochemistry, 43:2605-2612.
P.D. Coureux, A.L. Wells, J. Ménétrey, C.M. Yengo, C.A. Morris, H.L. Sweeney, A. Houdusse (2003). The myosin V motor visualized at 2.0Å without bound nucleotide reveals a new structural state of myosin. Nature, 425:419-23.
C.M. Yengo, E.M. De La Cruz, D. Safer, E.M. Ostap, H.L. Sweeney (2002). Kinetic characterization of the weak binding states of myosin V. Biochemistry, 41:8508-8517.
C.M. Yengo, E.M. De La Cruz, L. Chrin, C.L. Berger (2002). Actin-induced closure of the actin binding cleft of smooth muscle myosin. Journal of Biological Chemistry, 277:24114-24119.
C.M. Yengo, L. Chrin, A.S. Rovner, C.L. Berger (2000). Tryptophan 512 is sensitive to structural changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle. Journal of Biological Chemistry, 275:25481-25487.
C.M. Yengo, P.M. Fagnant, L. Chrin, A.S. Rovner, C.L. Berger (1998). Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface. Proceedings of the National Academy of Science, 95:12944-12940.
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Research Areas:
Cytoskeleton
Motor Proteins
Myosin
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