Molecular Dynamics Calculations of the Interaction Energy of Imidazole Glycerol Phosphate Dehydratase from Mycobacterium tuberculosis with Triazole Derivatives

Free energy changes upon the binding of three triazole derivatives in the active site of imidazole glycerol phosphate dehydratase from Arabidopsis thaliana and Mycobacterium tuberculosis were calculated by computer simulation. These data were correlated with the previously evaluated inhibition const...

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Bibliographic Details
Published in:Crystallography reports 2020, Vol.65 (5), p.755-756
Main Authors: Agapova, Yu. K., Komolov, A. S., Timofeev, V. I.
Format: Article
Language:English
Subjects:
Binding
Computer simulation
Crystallography and Scattering Methods
Dehydration
Derivatives
Enzymes
Free energy
Glycerol
Imidazole
Mathematical analysis
Molecular dynamics
Physics
Physics and Astronomy
Structure of Macromolecular Compounds
Triazoles
Tuberculosis
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Summary:Free energy changes upon the binding of three triazole derivatives in the active site of imidazole glycerol phosphate dehydratase from Arabidopsis thaliana and Mycobacterium tuberculosis were calculated by computer simulation. These data were correlated with the previously evaluated inhibition constants for the binding of these inhibitors with the enzyme from Arabidopsis thaliana . The free energy changes for both enzymes calculated by the MM-PBSA method correlate with the inhibition constants of the plant enzyme determined by experimental methods.
ISSN:1063-7745
1562-689X
DOI:10.1134/S1063774520050028