Center for Relativistic Laser Science

2018 GRC

Abstract

The UnaG protein and its a series of mutants can generate fluorescence through binding a ligand and its ligand binds to the protein through many noncovalent interactions. Although a difference between wild type and mutants is only single residue on N-terminus, they show significantly big change of fluorescence intensity. To elucidate the origin of fluorescence intensity changes, we carried out MD simulations for these UnaG series and found evidences that the changed environment and the encapsulated water makes more rigid motion of the ligand, which can lead higher quantum yield. And, our results revealed that these reasons are come from the higher stability of protein structure near the mutation site.