✦ LIBER ✦

A reinterpretation of paramagnetic line broadening in the nuclear magnetic resonance spectra of amino acids and peptides. I. The copper(II)-glycine system

✍ Scribed by Beattie, James K.; Fensom, Donald J.; Freeman, Hans C.

Book ID: 126398919
Publisher: American Chemical Society
Year: 1976
Tongue: English
Weight: 929 KB
Volume: 98
Category: Article
ISSN: 0002-7863
DOI: 10.1021/ja00418a029

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Contribution of minor species to paramag

Contribution of minor species to paramagnetic line broadening of proton nuclear magnetic resonance spectra in peptide-copper(II) system

✍ Kuroda, Yoshihiro; Aiba, Hiroji 📂 Article 📅 1979 🏛 American Chemical Society 🌐 English ⚖ 696 KB

Nuclear magnetic resonance studies of th

Nuclear magnetic resonance studies of the acid-base chemistry of amino acids and peptides. II. Dependence of the acidity of the C-terminal carboxyl group on the conformation of the C-terminal peptide bond

✍ Evans, Christopher A.; Rabenstein, Dallas L. 📂 Article 📅 1974 🏛 American Chemical Society 🌐 English ⚖ 719 KB

Influence of D and L amino-acid residues

Influence of D and L amino-acid residues on the conformation of peptides in solution: A carbon-13 nuclear magnetic resonance study of cyclo(prolyl-leucyl)

✍ Roxanne Deslauriers; Z. Grzonka; Roderich Walter 📂 Article 📅 1976 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 375 KB 👁 2 views

## Abstract The ^13^C chemical shifts and spin‐lattice relaxation times are reported for __cyclo__(L‐Pro‐L‐Leu) and __cyclo__(L‐Pro‐D‐Leu). The chemical shifts of the D and L leucyl residues in the cyclic peptides differ from each other by 1.8 and 3.6 parts per million for the α and β carbons, resp