Issue 22, 1979

Histidine residues of myoglobin studied by 1H nuclear magnetic resonance spectroscopy

Abstract

Titration curves of all the H-2 and H-4 resonances of the eleven titrating histidine residues in ferrous carbon monoxide sperm whale myoglobin are given; the H-4 resonance of the distal histidine has been observed at ca. 2·2 p.p.m. upfield of its normal position and on titration, the distal histidine resonances give a pK′ of 5·2 at 40 °C.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1979, 997-998

Histidine residues of myoglobin studied by 1H nuclear magnetic resonance spectroscopy

J. H. Bradbury, S. L. M. Deacon and M. D. Ridgway, J. Chem. Soc., Chem. Commun., 1979, 997 DOI: 10.1039/C39790000997

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