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1H and 13C NMR study of phosphopeptides: 2—Ac–PSer–Gly, Ala–PSer–Gly and Gly–PSer–Phe

✍ Scribed by L. Pogliani; D. Ziessow


Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
437 KB
Volume
22
Category
Article
ISSN
0749-1581

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✦ Synopsis


H and 13C NMR spectra of AC-PSer-Gly, Ala-PSer-Gly and Gly-PSer-Phe have been measured and analysed as a function of pD. The NMR parameters of the Beryl side chain are a function of the sequence. The second titration step of the phosphate group (pK, = 5.7) is much more difEcdt to detect in AcPSer-Gly and Ala-PSer-Gly than in Gly-PSer-Phe. The conformation in which H-a-C-a-C-&O-P forms a planar W-type arrangement predominates only for Ala-PSer-Gly. In the other two phosphopeptides the gauche conformations contribute increasingly, in particular for Gly-PSer-Phe.