Kinetics of Folding of Staphylococcal Nuclease

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<jats:p> Staphylococcal nuclease undergoes a reversible structural transition between <jats:italic>p</jats:italic> H3 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. </jats:p>

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  • Science

    Science 167 (3919), 886-887, 1970-02-06

    American Association for the Advancement of Science (AAAS)

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