The excited state dynamics of the blue fluorescent protein (BFP) and its variants, azurite, EBFP1.2, and EBFP2.0, are studied using molecular dynamics (MD) simulations on potential energy surfaces (PESs) generated with the interpolated mechanics-molecular mechanics (IM/MM) scheme. This IM/MM strategy adopts the interpolated PES for an important area of the complex and the conventional force field for the remaining part. We focus on the internal rotation dynamics of the chromophore unit, which is directly related to its fluorescence property, and analyze the time evolutions of the nonrotated chromophore fractions based on trajectories over 10 mu s of aggregate simulation time. The characteristics obtained from the calculated time progresses of the nonrotated chromophore fractions in BFP and other variants agree well with experimentally observed properties. The results show that the MD simulation with an IM/MM potential is an attractive approach for studying excited state dynamics of fluorescent proteins in consideration of its efficiency and reliability. We also attempt to investigate the detailed roles that the mutated residues play in delaying the excited state chromophore twisting and thus improving the fluorescence property, and discuss the contributions by the Coulombic and the steric interactions between the chromophore and the mutated residues.