Department of Biochemistry and Molecular Biophysics at Washington University School of Medicine in St. Louis, MO Washington University School of Medicine in St. Louis, MO Washington University in St. Louis, MO




Faculty



picture of scott mathews

F. Scott Mathews


Professor
Dept. of Biochemistry and
Molecular Biophysics

Office: 2210 Cancer Research
Phone: 314-362-1080
Fax: 314-362-7183
Email: mathews@biochem.wustl.edu

Lab Website
Research Opportunities

Mailing Address:
WUSM - Biochemistry Dept.
660 S. Euclid Ave., MS8231
St. Louis, MO 63110



Research Interests

X-ray structure and analysis of macromolecules



Selected Publications

  • Sukumar, N., Dewanti, A., Merli, A., Rossi, G.L., Mitra, B. and Mathews, F.S. Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr D Biol Crystallogr 65:543-552 (2009).
  • Hassan-Abadallah, A., Zhao, G., Chen, Z., Mathews, F.S. and Schuman Jorns, M. Arginine 49 is a bifunctional residue important in catalysis and biosynthesis of monomeric sarcosine oxidase: A context-sensitive model for the electrostatic impact of arginine to lysine mutations. Biochemistry 47:2913-2922 (2008).

  • Gandhi, P.S., Chen, Z., Mathews, F.S. and Di Cera, E. Structural identification of the pathway of long-range communication in an allosteric enzyme. Proc Natl Acad Sci U S A. 105:1832-1837 (2008).

  • Ma, J.K., Wang, Y., Carrell, C.J., Mathews, F.S. and Davidson, V.L. A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin(,). Biochemistry 46:11137-11146 (2007).

  • Carrell, C.J., Bruckner, R.C., Venci, D., Zhao, G., Jorns, M.S. and Mathews, F.S. NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: Structures of closed and open forms at 1.15 and 1.90 A resolution. Structure 15:928-941 (2007).

  • Bush-Pelc, L.A., Marino, F., Chen, Z., Pineda, A.O. Mathews, F.S. and Di Cera, E. Important role of the Cys-191: Cys-220 disulfide bond in thrombin function and allostery. J Biol Chem 282:27165-27170 (2007).

  • Bah, A., Chen, Z., Bush-Pelc, L.A., Mathews, F.S. and Di Cera, E. Crystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4. Proc Natl Acad Sci U S A. 104:11603-11608 (2007).

 

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