The oligosaccharide part of an N-linked triantennary glycopeptide from calf fetuin with fourteen carbohydrate residues and its smaller derivatives obtained by successive enzymic cleavage of the terminal residues were investigated using 2D 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) spectroscopy. As
✦ LIBER ✦
One- and two-dimensional 90.5-MHz 13C-NMR spectroscopy of the N-linked triantennary oligosaccharide units of calf fetuin
✍ Scribed by Elisha Berman; Peter Bendel
- Book ID
- 115918328
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 333 KB
- Volume
- 204
- Category
- Article
- ISSN
- 0014-5793
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A two-dimensional 1H-n.m.r. (500 MHz) an
✍
Elisha Berman; Ursula Dabrowski; Janusz Dabrowski
📂
Article
📅
1988
🏛
Elsevier Science
🌐
English
⚖ 1021 KB
Assignments of the 1H and 13C NMR spectr
✍
Dagfinn W. Aksnes; George W. Francis; Dionissios Papaioannou
📂
Article
📅
1993
🏛
John Wiley and Sons
🌐
English
⚖ 161 KB
## Abstract The ^1^H and ^13^C NMR spectra of __trans__‐4‐hydroxy‐__N__‐9‐fluorenylmethoxycarbonyl‐L‐proline show a 56:44 mixture of two conformers due to hindered rotation around the partial CN double bond. A combination of homo‐ and heteronuclear 1 D and 2D NMR techniques provided the assignment