Elucidating the Macromolecular Crowding Effects on Intracellular NADH and Enzyme Binding using Time-Resolved Associated Anisotropy

Abstract

performed a series of long molecular dynamics simulations for the SA or its mutants with/without biotin analog systems developed by kawato et al. to investigate the effect of mutations on the structural change, dynamics and the thermodynamic properties of the system. We also have calculated free energy of the systems using MPCAFEE method to evaluate binding affinity of artificial biotin analogs with SA mutants. We found that the mutations in the biotin-binding pocket affect not only the interaction with surrounding residues and with biotin analog, but also the tetramerization of the SA mutants.