Assignment of amino acids in peptides by correlation of α-hydrogen and carbonyl carbon-13 resonances
✍ Scribed by Chantal Wynants; Klaas Hallenga; Georges Van Binst; Alain Michel; Jacqueline Zanen
- Publisher
- Elsevier Science
- Year
- 1984
- Weight
- 304 KB
- Volume
- 57
- Category
- Article
- ISSN
- 0022-2364
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract A number of carbonyl‐bis‐(amino acid esters) have been examined by proton and carbon‐13 nuclear magnetic resonance techniques. All but one of the compounds were synthesized with two chiral centers of like‐configuration. In one series, the diastereotopic nonequivalence of isopropyl methy
A one-dimensiooal version of the heteronuclear multiple bond correlation experiment (HMBC) is shown to be an excellent alternative to the full two-dimensional experiment when the carbon resonances are well resolved. The quaternary resonances of larnbertellin, a metabolite of Ciboria gordonii Funk, a
Inverse heteronuclear shift correlation via long-range coupling to the carbonyl carbons of the cyclic hexapeptide cyclo(-Phe1\*-Thr'o-AIa9-Trps-Phe7-D-Pro6-) allows the sequential assignment of the amino acids. This experiment has a higher sensitivity than the conventional COLOC sequence.