Kinetics of folding of staphylococcal nuclease.

Staplhylococcal nuclease undergoes a reversible structural transition between (p)h3 and 4 which be mesured by changes in tryptoham fluorescence. A stopped-flow spectrofluorometer was used to study the kinetics 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.