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(a) The kinetics of unfolding and refolding for URN1-FF at pH 5.7 were followed by Trp intrinsic fluorescence. Stopped-flow experiments were performed at 298 K (circles) and 310 K (triangles). (b) Unfolding rates in 8 M urea at pH ranging from 3.5 to 6.5 were recorded at 310 K. The rate constants were measured under conditions of apparent two-state folding.
