PMID:10681466

Citation	Leeson, DT, Gai, F, Rodriguez, HM, Gregoret, LM and Dyer, RB (2000) Protein folding and unfolding on a complex energy landscape. Proc. Natl. Acad. Sci. U.S.A. 97:2527-32
Abstract	Recent theories of protein folding suggest that individual proteins within a large ensemble may follow different routes in conformation space from the unfolded state toward the native state and vice versa. Herein, we introduce a new type of kinetics experiment that shows how different unfolding pathways can be selected by varying the initial reaction conditions. The relaxation kinetics of the major cold shock protein of Escherichia coli (CspA) in response to a laser-induced temperature jump are exponential for small temperature jumps, indicative of folding through a two-state mechanism. However, for larger jumps, the kinetics become strongly nonexponential, implying the existence of multiple unfolding pathways. We provide evidence that both unfolding across an energy barrier and diffusive downhill unfolding can occur simultaneously in the same ensemble and provide the experimental requirements for these to be observed.
Links	PubMed PMC15962 Online version:10.1073/pnas.040580397
Keywords	Bacterial Proteins/chemistry; Escherichia coli/chemistry; Kinetics; Models, Chemical; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry, Infrared; Temperature; Thermodynamics; Time Factors
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