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Issue 1, 2016
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Theoretical studies of energetics and binding isotope effects of binding a triazole-based inhibitor to HIV-1 reverse transcriptase

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Abstract

Understanding of protein-ligand interactions is crucial for rational drug design. Binding isotope effects, BIEs, can provide intimate details of specific interactions between individual atoms of an inhibitor and the binding pocket. We have applied multi-scale QM/MM simulations to evaluate binding energetics of a novel triazole-based non-nucleoside inhibitor of HIV-1 reverse transcriptase and to calculate associated BIEs. The binding sites can be distinguished based on the 18O-BIE.

Graphical abstract: Theoretical studies of energetics and binding isotope effects of binding a triazole-based inhibitor to HIV-1 reverse transcriptase

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Publication details

The article was received on 08 Oct 2015, accepted on 20 Nov 2015 and first published on 20 Nov 2015


Article type: Paper
DOI: 10.1039/C5CP06050H
Citation: Phys. Chem. Chem. Phys., 2016,18, 310-317
  • Open access: Creative Commons BY license
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    Theoretical studies of energetics and binding isotope effects of binding a triazole-based inhibitor to HIV-1 reverse transcriptase

    A. Krzemińska, K. P. Świderek and P. Paneth, Phys. Chem. Chem. Phys., 2016, 18, 310
    DOI: 10.1039/C5CP06050H

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