Reports

Kinetics of Folding of Staphylococcal Nuclease

Science  06 Feb 1970:
Vol. 167, Issue 3919, pp. 886-887
DOI: 10.1126/science.167.3919.886

Abstract

Staplhylococcal nuclease undergoes a reversible structural transition between ph3 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.

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