Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, XI. Characterization of Selectively Deuterated Analogs of Staphylococcal Nuclease
- 1 February 1970
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 65 (2) , 395-401
- https://doi.org/10.1073/pnas.65.2.395
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.Keywords
This publication has 3 references indexed in Scilit:
- Staphylococcal nuclease (Foggi strain). I. Order of cyanogen bromide fragments and a "fourth" histidine residue.1968
- High-Resolution Nuclear Magnetic Resonance Spectra of Selectively Deuterated Staphylococcal NucleaseScience, 1968
- Catalytic Properties and Specificity of the Extracellular Nuclease of Staphylococcus aureusJournal of Biological Chemistry, 1967