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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Feb;65(2):395–401. doi: 10.1073/pnas.65.2.395

Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, XI. Characterization of Selectively Deuterated Analogs of Staphylococcal Nuclease

I Putter 1, J L Markley 1, O Jardetzky 1
PMCID: PMC282916  PMID: 4984238

Abstract

The preparation of five different selectively deuterated analogs of the enzyme staphylococcal nuclease has been previously reported.1-3 The five selectively deuterated enzymes have full enzymatic activity with DNA and RNA substrates and identical amino acid compositions; and they all appear to have similar conformations in solution, despite their very different hydrogen/deuterium contents.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cuatrecasas P., Fuchs S., Anfinsen C. B. Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus. J Biol Chem. 1967 Apr 10;242(7):1541–1547. [PubMed] [Google Scholar]
  2. Cusumano C. L., Taniuchi H., Anfinsen C. B. Staphylococcal nuclease (Foggi strain). I. Order of cyanogen bromide fragments and a "fourth" histidine residue. J Biol Chem. 1968 Sep 25;243(18):4769–4777. [PubMed] [Google Scholar]
  3. Markley J. L., Putter I., Jardetzky O. High-resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease. Science. 1968 Sep 20;161(3847):1249–1251. doi: 10.1126/science.161.3847.1249. [DOI] [PubMed] [Google Scholar]

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