PMID: 6962Jun 1, 1976

Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance

Proceedings of the National Academy of Sciences of the United States of America
H Shindo, J S Cohen


Several of the carboxyl carbon atom resonances of hen egg-white lysozyme (mucopeptide N-acetylmuramoyl hydrolase, EC have been resolved by 13C-nuclear magnetic resonance (NMR) at 68 MHz. The change in chemical shift of the carboxyl carbon atom resonances, as a function of pH, has enabled the distinction of these resonances against the background of many nontitrating carbonyl group resonances. Several apparent microscopic ionization constants have been determined from the carboxyl group NMR titration curves, and possible assignments are discussed. Preliminary experiments were carried out in the presence of cobaltous ion, and selective shifts of several resonances were observed. Our results indicate the possibility of the direct observation of a wide range of single functional groups of proteins in solution by NMR techniques.


Jan 15, 1973·European Journal of Biochemistry·M H FreedmanJ S Cohen
Jan 23, 1974·Journal of the American Chemical Society·A R QuirtM H Freedman
May 23, 1972·Biochemistry·C Tanford, R Roxby
Jun 28, 1972·Journal of the American Chemical Society·M Christl, J D Roberts
Oct 1, 1967·Proceedings of the National Academy of Sciences of the United States of America·D H MeadowsO Jardetzky
Apr 10, 1969·Biochemical and Biophysical Research Communications·C C McDonald, W D Phillips


Nov 3, 2007·Biochimica Et Biophysica Acta·Vipin AgarwalBernd Reif
Jul 1, 1990·International Journal of Peptide and Protein Research·M BernardP Jollès
Jan 1, 1978·CRC Critical Reviews in Biochemistry·J S Cohen

Related Concepts

Carboxylic Acids
Hydrogen-Ion Concentration
In Vivo NMR Spectroscopy
Protein Conformation

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