31 P nuclear magnetic resonance spectroscopy of the phosphorylated tetrapeptide GlyGlyAspAla | Zendy

Schlemmer Heinz | Zendy; Sontheimer Gerhard M. | Zendy; Kalbitzer Hans Robert | Zendy

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31 P nuclear magnetic resonance spectroscopy of the phosphorylated tetrapeptide GlyGlyAspAla

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).

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