Kinetics of folding of staphylococcal nuclease

Abstract

Staphylococcal nuclease undergoes a reversible structural transition between pH 3 and 4 which can be measured by changes in tryptophan fluorescence. A stopped-flow spectrofluorometer was used to study the kinetics of renaturation of nuclease from the acidified form on neutralization. The refolding is fast, and the data can be described as a sequence of two first-order processes, with half times of about 55 and 350 milliseconds, respectively.