✦ LIBER ✦
The effect of phosphorylation of the histidyl residue in the tetrapeptide Gly-Gly-His-Ala. Changes of chemical shift and pK values in 1H- and 31P-NMR spectra
✍ Scribed by Hans Robert Kalbitzer; Paul Rösch
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 362 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0749-1581
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Phosphorylation of the tetrapeptide Gly‐Gly‐His‐Ala by phosphoamidate provides a model peptide for proteins which, in the course of their reaction, bind a phosphoryl group to an imidazole ring. ^31^P‐ and ^1^H‐NMR data, including chemical shift and pK values, for this peptide and its three phospho‐derivatives are presented. These data show that it is possible, by NMR studies, to decide whether or not a peptide or a protein is phosphorylated at the N‐1 or at the N‐3 position of an imidazole ring, and how this information can be achieved.