## Abstract The ^17^O chemical shifts of the α‐carboxyl groups of the protein amino acids, including 4‐hydroxyproline, sarcosine and __N,N__‐dimethylglycine, were measured at 40°C in aqueous solution at variable pH (^17^O enrichment 10 atom‐%). The chemical shifts of the amino acids were found to b
17O NMR studies of the effect of mixed ligands on the bound water in aqueous solutions of amino acids and Co(II)
✍ Scribed by Efstathios D. Gotsis; Daniel Fiat
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 524 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0749-1581
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## Abstract The ^17^O‐NMR. line widths of the enriched amino acids glycine, aspartic acid, glutamic acid and, for comparative reasons, acetic acid were measured in aqueous solution between pH 1 and 14. The ^17^O‐NMR. line‐width maxima of glycine at pH≈︁11 and acetic acid at pH≈︁5 are shown to arise
## Abstract The study of protein hydration by time‐domain NMR is complicated by the great number of interactions involved, resulting from the presence of several amino acids and the possible modifications produced by the various structures. Moreover, a good comprehension of the molecular interactio
## Synopsis The synthesis of Leu-enkephalin selectively l70-enriched in Gly' and Gly3 is reported. The 170-nm chemical shifts of Leu5]-and [170-Gly3, Le~~l-enkephalins in H,O are almost identical and independent of the pH. Since hydrogen bonding is the dominant factor governing the chemical shifts