抄録
Time-resolved transient hole-burning (TRTHB) spectroscopy is quite effective to elucidate the conformational fluctuation dynamics of protein in ns-ms time regime, which has not been investigated intensively so far. It has also great importance for the understanding of the molecular-level mechanism of protein functioning. TRTHB study on Zn-substituted myoglobin has clarified its highly non-exponential fluctuation dynamics. The time scale of the observed fluctuation is distributed over very wide range from ns to μs. The results underscore the utility of the present method to characterize conformational dynamics of protein.
