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A transient kinetic procedure was used in examining the catalytic efficiency during single nucleotide incorporation of the M184V mutant of HIV-1 reverse transcriptase (RT). HIV-1 viral resistance is triggered when an amino acid substitution from methionine-184 to valine evokes the 1000-fold 3TC. Results indicate that the fidelity in M184V RT increases by a maximum of 2.4 times over the wild-type HIV-1 RT. Both the wild-type and 3TC-resistant mutant RT have higher fidelity when using an RNA template.

Research was conducted to examine the kinetics for the incorporation of dCMP, ddCMP and (+)SddCMP and its unnatural beta-L-(-) enantiomer, (-)SdCMP, into DNA/DNA and DNA/RNA primer-templates catalyzed by HIV-1 RT. The objective was to gain an insight into the differences between RNA-dependent and DNA-dependent polymerization. Results suggest that perturbations on the ribose ring of cytidine analogues decrease the rate and efficiency of incorporation but improves the binding affinity.