Students:
Fayyaz Younas, State University of New York at Stony Brook
Soumya Raychaudhuri, State University of New York at Buffalo
Advisors:
Daniel Ripoll, Cornell Theory Center
Carlos Faerman, Cornell University
Andrew Karplus, Cornell University
Abstract: The electrostatic properties of a/b barrel enzymes were studied by examining a subset of six enzymes containing this domain: triose phosphate isomerase, fructose-1,6-bisphosphatase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase. The electrostatic characteristics were determined computationally from crystallographic data. Generally, there is a highly positive area in front of the C-terminal side of the barrel, in the region where the active site is located. The backbone of the
a/b barrel domain was found to have a basic dipole that is preserved and modified in the actual enzymes.
S. Raychaudhuri, F. Younas, P.A. Karplus, C.H. Faerman and D.R. Ripoll. (1997). “Backbone Makes a Significant Contribution to the Electrostatics of α/β Barrel Proteins.” Protein Sci. 6, 1849-1857. [pdf]