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Digitale Medien

1H NMR study of casein phosphopeptide (1-25): Assignment and conformation (1991)

Tsuda, Sakae ; Niki, Ryoya ; Kuwata, Tamotsu ; [weitere]

Chichester : Wiley-Blackwell

Organic Magnetic Resonance 29 (1991), S. 1097-1102

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Details

ISSN: 0749-1581

Schlagwort(e): 1H NMR ; Casein phosphopeptide ; 2D NMR ; COSY ; HOHAHA ; NOESY ; β-Turn ; Chemistry ; Analytical Chemistry and Spectroscopy

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Chemie und Pharmazie

Notizen: The solution conformation of β-casein phosphopeptide (CPP) was studied by 1H NMR spectroscopy. As a prerequisite to the conformational analysis the spectral assignment was carried out for CPP in the Ca2+-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.

Zusätzliches Material: 3 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrc.1260291105

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