Exploring the free energy landscape of the folding and the intermediate ensemble of globular proteins.

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The folding mechanisms of two globular proteins, staphylococcal nuclease and horse apomyoglobin, were investigated by using the ultrarapid mixing technique combined with the mutation analysis. Staphylococcal nuclease molecules were found to be already compact within the β-barrel domain several millisecond after the initiation of the folding reaction. Apomyoglobin accumulated at least one intermediate 100 microseconds after the initiation of the folding reaction, followed by the accumulation of at least two intermediate in the sequential pathway, before reaching the native state.