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1 H NMR study of casein phosphopeptide (1–25): Assignment and conformation
Author(s) -
Tsuda Sakae,
Niki Ryoya,
Kuwata Tamotsu,
Tanaka Isao,
Hikichi Kunio
Publication year - 1991
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.1260291105
Subject(s) - chemistry , phosphopeptide , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , peptide , biochemistry
Abstract The solution conformation of β‐casein phosphopeptide (CPP) was studied by 1 H NMR spectroscopy. As a prerequisite to the conformational analysis the spectral assignment was carried out for CPP in the Ca 2+ ‐free and ‐bound states by the use of two‐dimensional NMR spectroscopy. The assigned resonances were used for (1) pH‐titration experiments, (2) elucidation of the temperature dependence of the amide resonance and (3) a nuclear Overhauser enhancement (NOE) experiment. Although the β‐turn conformation is predicted for the sequence – Val8–Pro9–Gly10–Glu11–of CPP, the present NMR results do not provide favourable evidence for its formation.