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pubmed-article:15084137pubmed:abstractTextThe effect of the K103N mutation of HIV-1 reverse transcriptase (RT) on the activity of efavirenz analogues was studied via Monte Carlo/free energy perturbation calculations. The relative fold resistance energies indicate that efavirenz binds to K103N RT in a manner similar to the wild-type enzyme. The improved performance of the quinazolinones against the mutant enzyme is attributed to formation of a more optimal hydrogen-bonding network with bridging water molecules between the ligands and Glu138.lld:pubmed
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pubmed-article:15084137pubmed:articleTitleStructural and energetic analyses of the effects of the K103N mutation of HIV-1 reverse transcriptase on efavirenz analogues.lld:pubmed
pubmed-article:15084137pubmed:affiliationDepartment of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.lld:pubmed
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