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31 P nuclear magnetic resonance spectroscopy of the phosphorylated tetrapeptide GlyGlyAspAla
Author(s) -
Schlemmer Heinz,
Sontheimer Gerhard M.,
Kalbitzer Hans Robert
Publication year - 1988
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260260315
Subject(s) - chemistry , tetrapeptide , nuclear magnetic resonance spectroscopy , alanine , spectroscopy , phosphate , peptide , phosphorylation , nuclear magnetic resonance , stereochemistry , amino acid , organic chemistry , biochemistry , physics , quantum mechanics
The model peptide glycylglycylaspartylalanine was phosphorylated in the NMR sample tube and characterized by 31 P NMR spectroscopy. The p K a2 value of the acyl phosphate group in glycylglycyl(β‐aspartyl phosphate)alanine was determined to be 4.6 and the chemical shift was −6.45 ppm at low pH (1.5) and −1.27 ppm at high pH (8.0).