@misc{oai:repo.qst.go.jp:00079062,
 author = {Sakuraba, Shun and Sakuraba, Shun},
 month = {Feb},
 note = {The free-energy difference of two physicochemical states is an essential value describing the stability of the molecules. In the context of protein engineering, the free-energy changes upon mutations can answer whether the protein is stabilized or destabilized upon mutations.Developments in molecular dynamics simulation, combined with the growth of the computational power in the recent computer hardware,provides us a way to predict the free-energy difference of proteins upon mutations at a cost of moderate computational requirements.We reimplemented a state-of-the-art free-energy estimation method for protein mutations, FEP/REST (free energy perturbation /replica exchange with solute tempering) and its improvements on a molecular dynamics software GROMACS. We evaluated its prediction capability by comparing it with experimental measurements. Accuracies, parameter choices and extensions will be discussed., 2020 Biophysical Society Annual Meeting},
 title = {A COMPUTATIONAL STUDY OF FREE-ENERGY CHANGES UPON PROTEIN MUTATIONS},
 year = {2020}
}