@misc{oai:repo.qst.go.jp:00080520,
 author = {Taguchi, Masahiko and Oyama, Ryo and Kaneso, Masahiro and Hayashi, Shigehiko and Taguchi, Masahiko},
 month = {Sep},
 note = {HIV-1 protease is a target of drug development and various inhibitors binding to two Asps in the catalytic site were developed. However, it has a serious drug-resistance, that is, some mutations cause existing inhibitors ineffective, even though hydrolysis reaction of substrate proceeds. To resolve the drug-resistance problem, it is important to clarify difference of recognition mechanism of the protease for inhibitors in the case of native and drug resistance mutational structures, respectively. For indinavir, it is known that mutation (V82T/I84V) greatly affects its binding free energy to HIV-1 protease. We performed QM/MM free energy calculations, and succeeded to determine the protonated states of catalytic Asps and the relative binding free energy., 第58回日本生物物理学会年会},
 title = {Free Energy Calculations of HIV-1 Protease Binding Indinavir and Its Drug-Resistant Mutant},
 year = {2020}
}