Kinetics of Folding of Staphylococcal Nuclease
- 6 February 1970
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 167 (3919), 886-887
- https://doi.org/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.Keywords
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