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Issue 5, 2001
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Ab initio study of the physical nature of interactions between enzyme active site fragments invacuo

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Abstract

A recently developed direct version of variation–perturbation decomposition of intermolecular interaction energy into electrostatic, exchange, delocalization and correlation components has been used to explore the physical nature of interactions between key fragments of several enzyme active sites and corresponding reactants or inhibitors in [italic v (to differentiate from Times ital nu)]acuo. Despite neglecting solvent effects our results correlate reasonably with available experimental data and indicate the dominant electrostatic nature of inhibitory effects of PheP derivatives in leucine aminopeptidase and pKa shifts resulting from amino acid substitutions in mutated subtilisins. The range of applicability of the electrostatic approximation has been examined for the chorismate mutase enzyme.

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Publication details

The article was received on 08 Sep 2000, accepted on 20 Dec 2000 and first published on 22 Jan 2001


Article type: Paper
DOI: 10.1039/B007280J
Citation: Phys. Chem. Chem. Phys., 2001,3, 657-663
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    Ab initio study of the physical nature of interactions between enzyme active site fragments invacuo

    W. Andrzej Sokalski, P. Kȩdzierski and J. Grembecka, Phys. Chem. Chem. Phys., 2001, 3, 657
    DOI: 10.1039/B007280J

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