| Comments |
P. R87 left column bottom paragraph to p.R87 right column 2nd paragraph: "What structural, thermodynamic or kinetic features determine whether a protein folds through a stable intermediate state? Table 2 summarises the kinetic and thermodynamic data for folding for some of the proteins that have been shown to fold to their native states via a populated intermediate ([primary sources 54–63], F. Rousseau, J.W.H. Schymkowitz, M. Sénchez del Pino and L.S. Itzhaki, unpublished observations). This is not a comprehensive list of proteins with multi-state kinetics, but includes those proteins for which there is data available on the denaturant dependence of the unfolding and refolding rates. For a more comprehensive discussion of intermediate states in protein folding see recent reviews [refs 64–67]. Neither the rates of folding, 0.5–900/s, nor the position of the rate-limiting transition state, βT = 0.6–0.9, nor the topological complexity of the native fold (as measured by the contact order), are significantly different for the proteins listed in Table 2 from those which fold with two-state kinetics, Table 1. The main differences appear to be chain length and stability." See notes beneath table |