Summary
This is the last in a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3′-nucleotidohydrolase, EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses the use of the nuclease as a model system for the study of the mechanisms and energetics of the folding-unfolding reaction in proteins and for the study of the interrelationships between amino acid sequence and three-dimensional structure.
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This article is the last in a series of four devoted to the staphylococcal nuclease. The previous articles have discussed its isolation and enzymology, the chemical and enzymological studies of its active site and the high-resolution crystallographic work. The third article also put forth a mechanism for the enzymatic reaction based on the nuclease's known chemical and structural properties. Work from this laboratory has been supported by grants from the National Institute of General Medical Sciences, N.I.H. and the Robert A. Welch Foundation to F. A. Cotton and from the Welch Foundation to E. E. Hazen, Jr.
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Tucker, P.W., Hazen, E.E. & Cotton, F.A. Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology. Mol Cell Biochem 23, 131–141 (1979). https://doi.org/10.1007/BF00219452
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DOI: https://doi.org/10.1007/BF00219452