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PMID: 5673435 Published · ppublish English Journal Article

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

Science (New York, N.Y.) ·Vol. 161 ·No. 3847 ·1968-09-20 ·Pages 1249-51

Markley JL, Putter I, Jardetzky O

Abstract

An analog of staphylococcal nuclease has been prepared in which all amino acids, except the six following, are fully deuterated: tryptophan; methionine; tyrosine, in ring positions 2 and 6; histidine, in ring position 2; aspartic acid and asparagine, beta-methylene; and glutamic acid and glutamine, gamma-methylene. The analog has a much simpler high-resolution nuclear magnetic resonance spectrum than the fully protonated enzyme. The effects of calcium ion and of the inhibitor 3', 5'-thymidine diphosphate on the spectrum of the analog were readily detected.

MeSH Terms
Amino Acids/analysis Asparagine Aspartic Acid Calcium Deoxyribonucleases/analysis Deuterium Glutamates Glutamine Histidine Magnetic Resonance Spectroscopy Methionine Nucleotides Ribonucleases/analysis Staphylococcus Tryptophan Tyrosine
Chemicals
Amino Acids Glutamates Nucleotides Glutamine Aspartic Acid Tyrosine Histidine Asparagine Tryptophan Methionine Deuterium Deoxyribonucleases Ribonucleases Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Markley J L
Putter I
Jardetzky O
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1968-09-20
Pages
1249-51
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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