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Science 6 February 1970:
Vol. 167. no. 3919, pp. 886 - 887
DOI: 10.1126/science.167.3919.886
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Articles

Kinetics of Folding of Staphylococcal Nuclease

Alan N. Schechter 1, Raymond F. Chen 1, and Christian B. Anfinsen 1

1 National Inistitiutes of Health, Bethesda, Maryland 20014

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Some Aspects of the Structure of Staphylococcal Nuclease: PART I. CRYSTALLOGRAPHIC STUDIES.
F. A. Cotton, C. J. Bier, V. W. Day, E. E. Hazen Jr., and S. Larsen (1972)
Cold Spring Harb Symp Quant Biol 36, 243-255
   Abstract »    PDF »
Some Aspects of the Structure of Staphylococcal Nuclease PART II. STUDIES IN SOLUTION.
C. B. Anfinsen, A. N. Schechter, and H. Taniuchi (1972)
Cold Spring Harb Symp Quant Biol 36, 243-255
   Abstract »    PDF »
Measurement of Fast Biochemical Reactions: Flow and relaxation methods are being used to study chemical processes in biological macromolecules.
A. N. Schechter (1970)
Science 170, 273-280
   Abstract »    PDF »


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