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1H NMR study of casein phosphopeptide (1–25): Assignment and conformation

✍ Scribed by Sakae Tsuda; Ryoya Niki; Tamotsu Kuwata; Isao Tanaka; Kunio Hikichi

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
451 KB
Volume
29
Category
Article
ISSN
0749-1581

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✦ Synopsis

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.

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