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Proton magnetic resonance studies of the tyrosine residues of staphylococcal nuclease using [3,5- 2H 2]tyrosine
Journal article   Peer reviewed

Proton magnetic resonance studies of the tyrosine residues of staphylococcal nuclease using [3,5- 2H 2]tyrosine

Jack S. Cohen, Marvin Feil and Irwin M. Chaiken
Biochimica et biophysica acta. Protein structure, v 236(2), pp 468-478
1971
DOI: https://doi.org/10.1016/0005-2795(71)90227-3
PMID: 5569481

Abstract

tetramethylsilane proton magnetic resonance TMS PMR
A staphylococcal nuclease analogue, [3,5- 2H 2]tyrosyl nuclease, was prepared containing all seven tyrosine residues deuterated in the positions ortho to the hydroxyl group. Each tyrosine residue in this analogue gives a singlet resonance in the aromatic region of the proton magnetic resonance spectrum, as found for [3,5- 2H 2]tyrosine itself, resulting in a partially simplified aromatic spectrum. [3,5- 2H 2]Tyrosyl nuclease was selectively nitrated with tetranitromethane in the presence of Ca 2+ and the inhibitor, deoxythymidine 3′,5′-diphosphate, ( Cuatrecasas et al., J. Biol. Chem., 243 (1968) 4787), to produce the 3-nitrotyrosyl-115 derivative, which was purified by affinity chromatography. Several differences between the PMR spectra of [3,5- 2H 2]tyrosyl nuclease and [3-nitrotyrosyl-115]-[3,5- 2H 2]tyrosyl nuclease are observed. Based on knowledge of the spectra of [3,5- 2H 2]-tyrosine and its 3-nitro derivative, it appears that the differences correspond to shifts of at least two tyrosine resonances. It is suggested that substitution at tyrosine-115 results in a chemical shift for at least one adjacent tyrosine residue. Tentative resonance assignments are made based on present knowledge of the chemistry and structure of nuclease.

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