A Molecular Dynamics Study of Michaelis Complex for Designing Selective Transition State Analog Inhibitors for Cysteine Protease calpain-2

Abstract

sampling (REUS) molecular dynamics simulations [2]. REUS is a powerful conformational sampling method to overcome energy barriers. We applied this method to the HDAC3-T247 system and HDAC2-T247 system. These have very similar amino-acid sequences and similar structures. From results of these simulations, we obtained free energy landscapes. The results of these calculations show that the docked state is the most stable in the HDAC3-T247 system but in the HDAC2-T247 system, the docked state is less stable than undocked states. These results agree with experimental data. In this poster, we present these results. References:[1] T.