A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.
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Hosszu, L., Craven, C., Parker, M. et al. Structure of a kinetic protein folding intermediate by equilibrium amide exchange. Nat Struct Mol Biol 4, 801–804 (1997). https://doi.org/10.1038/nsb1097-801
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DOI: https://doi.org/10.1038/nsb1097-801
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