Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.
- 1 June 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (6) , 1979-1983
- https://doi.org/10.1073/pnas.73.6.1979
Abstract
Several of the carboxyl C atom resonances of hen egg-white lysozyme (mucopeptide N-acetylmuramoyl hydrolase, EC 3.2.1.17) were resolved by 13C-NMR at 68 MHz. The change in chemical shift of the carboxyl C atom resonances, as a function of pH, enabled the distinction of these resonances against the background of many nontitrating carbonyl group resonances. Several apparent microscopic ionization constants were determined from the carboxyl group NMR titration curves, and possible assignments are discussed. Preliminary experiments were carried out in the presence of Co2+, and selective shifts of several resonances were observed. The direct observation of a wide range of single functional groups of proteins in solution may be possible by NMR techniques.This publication has 19 references indexed in Scilit:
- Proposed rigidity of staphylococcal protease. CommentsBiochemistry, 1975
- The Mechanism of Water‐Proton Relaxation in Enzyme · Paramagnetic‐Ion ComplexesEuropean Journal of Biochemistry, 1974
- Carbon-13 nuclear magnetic resonance titration shifts in amino acidsJournal of the American Chemical Society, 1974
- Carbon‐13 Nuclear‐Magnetic‐Resonance Studies on Selected Amino Acids, Peptides, and ProteinsEuropean Journal of Biochemistry, 1973
- Nuclear magnetic resonance spectroscopy. Carbon-13 chemical shifts of small peptides as a function of pHJournal of the American Chemical Society, 1972
- Interpretation of protein titration curves. Application to lysozymeBiochemistry, 1972
- Proton Magnetic Resonance Studies at 220 MHz of the Histidine Residues of Staphylococcal NucleaseNature, 1970
- Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25°Biochemistry, 1969
- Perturbation of the PMR spectrum of lysozyme by Co+2Biochemical and Biophysical Research Communications, 1969
- Nuclear magnetic resonance studies of the structure and binding sites of enzymes. I. Histidine residues.Proceedings of the National Academy of Sciences, 1967