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.
D004798:Enzymes / Q000032:analysis*; D005453:Fluorescence; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010455:Peptides / Q000032:analysis; D011489:Protein Denaturation; D013053:Spectrophotometry; D013210:Staphylococcus / Q000201:enzymology*
D004798:Enzymes; D010455:Peptides