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The effect of phosphorylation of the histidyl residue in the tetrapeptide Gly‐Gly‐His‐Ala. Changes of chemical shift and pK values in 1 H‐ and 31 P‐NMR spectra
Author(s) -
Kalbitzer Hans Robert,
Rösch Paul
Publication year - 1981
Publication title -
organic magnetic resonance
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0030-4921
DOI - 10.1002/mrc.1270170203
Subject(s) - tetrapeptide , imidazole , chemistry , peptide , phosphorylation , residue (chemistry) , ring (chemistry) , stereochemistry , chemical shift , biochemistry , organic chemistry
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.