Journal
JOURNAL OF CHEMICAL PHYSICS
Volume 117, Issue 24, Pages 11024-11032Publisher
AMER INST PHYSICS
DOI: 10.1063/1.1521159
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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 mus-10 s, offering new clues for understanding energy landscape of proteins, as well as the structural and chemical dynamics therein. (C) 2002 American Institute of Physics.
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