Faculty

Key Words: Protein Interactions; Crystallography Computational Chemistry

Extensive studies of protein interactions and applications of computation to problems of biological structure. Developed Fast Fourier Transform methods for crystallographic computations, and helped solve the structure of human deoxyhemoglobin to high resolution. Participated extensively in the determination of the structures of a number of proteins and numerous mutated or chemically modified variants of these. Analysis of the structure of the cAMP dependent protein kinase and related structures. Prediction and theoretical analysis of protein-protein interactions. Computational analysis of signal transduction pathways and physiological systems.

SELECTED PUBLICATIONS:

Zheng, J., Trafny, E.A., Knighton, D.R., Xuong, N-h., Taylor, S.S., TenEyck, L.F. and Sowadski, J.M. Crystal structure of the catalytic subunit of CAMP-dependent protein kinase complexed with NMATP and inhibitor. Acta Cryst. D49:362-365, 1993.

Knighton, D.R., Cadena, D.L., Zheng, J., Ten Eyck, L.F., Taylor, S.S., Sowadski, J.M. and Gill, G.N. Structural features that specify tyrosine activity deduced from homology modeling of the EGF receptor. Proc. Natl. Acad. USA 90:5001-5005, 1993.

Zheng, J., Knighton, D.R., Xuong, N-h., Taylor, S.S., Sowadski, J.M. and Ten Eyck, L.F. Crystal structures of catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Prot. Sci. 2:1559-1573, 1993.

Su, Y., Dostmann, W.R.G., Herberg, F.W., Durick, K., Xuong, N.-h., Ten Eyck, L.F., Taylor, S.S. and Varughese, K.I. Regulatory (R1a) subunit of cAMP-dependent protein kinase: Crystal structure of a 1-91 deletion mutant defines cooperative CAMP binding sites. Science 269:807-813, 1995.

Ten Eyck, L.F., Mandell, J., Roberts, V.A. and Pique, M.E. Surveying molecular Interactions with DOT. In: Supercomputing '95, IEEE Press (1995).