Single-molecule approach to dispersed kinetics and dynamic disorder: Probing conformational fluctuation and enzymatic dynamics

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Abstract
This article reviews our efforts in understanding dynamical fluctuations of both conformation and enzymatic reactivity in single biomolecules. The single-molecule approach is shown to be particularly powerful for studies of dispersed kinetics and dynamic disorder. New single-molecule observations have revealed conformational transitions occurring on a broad range of timescales, 100 μs–10 s, offering new clues for understanding energy landscape of proteins, as well as the structural and chemical dynamics therein.