We have documented the folding pathway of the 10-kDa protein barstar from the first few microseconds at the resolution of individual residues from its well character- ized denatured state. The denatured state had been shown from NMR to have flickering native-like structure in the first two of its four α-helices. φ-value analysis shows that the first helix becomes substantially consolidated as the intermediate is formed in a few hundred microseconds, as does the second to a lesser extent. A native-like structure then is formed in a few hundred milliseconds as the whole structure consolidates.
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