Literature DB >> 4984238

Nuclear magnetic resonance studies of the structure and binding sites of enzymes. XI. Characterization of selectively deuterated analogs of staphylococcal nuclease.

I Putter, J L Markley, O Jardetzky.   

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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Year:  1970        PMID： 4984238      PMCID： PMC282916          DOI： 10.1073/pnas.65.2.395

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  3 in total

1.  Catalytic properties and specificity of the extracellular nuclease of Staphylococcus aureus.

Authors:  P Cuatrecasas; S Fuchs; C B Anfinsen
Journal:  J Biol Chem       Date:  1967-04-10       Impact factor: 5.157

2.  Staphylococcal nuclease (Foggi strain). I. Order of cyanogen bromide fragments and a "fourth" histidine residue.

Authors:  C L Cusumano; H Taniuchi; C B Anfinsen
Journal:  J Biol Chem       Date:  1968-09-25       Impact factor: 5.157

3.  High-resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease.

Authors:  J L Markley; I Putter; O Jardetzky
Journal:  Science       Date:  1968-09-20       Impact factor: 47.728
  3 in total
  3 in total

Review 1.  Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. IV. The nuclease as a model for protein folding.

Authors:  P W Tucker; E E Hazen; F A Cotton
Journal:  Mol Cell Biochem       Date:  1979-02-09       Impact factor: 3.396

2.  Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts.

Authors:  S Massou; V Puech; F Talmont; P Demange; N D Lindley; M Tropis; A Milon
Journal:  J Biomol NMR       Date:  1999-07       Impact factor: 2.835

3.  Nuclear magnetic resonance studies of the structure and binding sites of enzymes. XII. A conformational equilibrium in staphylococcal nuclease involving a histidine residue.

Authors:  J L Markley; M N Williams; O Jardetzky
Journal:  Proc Natl Acad Sci U S A       Date:  1970-03       Impact factor: 11.205
  3 in total

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