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Ya. I. Dobrogorskaya, A. V. Nemukhin
Simulation of the substrate
acylation in the active center of serine proteases
Abstract
Ab initio quantum chemistry calculations of the acylation stage of
hydrolysis of peptide bonds catalyzed by serine proteases have been carried
out. Construction of the potential energy surface for the model system and
location of the stationary points (minima and transition states) has been
performed by using the Hartree-Fock method with the Stevens-Bash-Krauss (SBK)
effective core potentials and the corresponding basis sets. The obtained energy
differences have been recalculated at the RHF/6-31+G*//RHF/SBK and
B3LYP-6-31+G*//RHF/SBK levels. It is shown that theoretical data correlate well
with the experimental results and elucidate details of the reaction mechanism.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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