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Title: Charge relay at the peptide bond. A proton magnetic resonance study of solvation effects on the amide electron density distribution. [Alumichrome and alumichrome C]

Journal Article · · J. Am. Chem. Soc.; (United States)
DOI:https://doi.org/10.1021/ja00849a040· OSTI ID:7365395

The proton magnetic resonance (/sup 1/H NMR) manifestations of amide solvation in polypeptides have been studied using alumichrome and alumichrome C as model compounds. The extreme structural rigidity of the alumichromes allowed the investigation to center on the chemical shifts of the amides as conformational drifts are precluded. The data have been analyzed primarily in terms of two main events: H bonding of the amide nitrogen to basic solvents (Me/sub 2/SO, DMF, and pyridine), and protonation of the amide carbonyl by Bronsted acids (chloroform, TFE, and TFA). The two solvent types cause a low-field shift of the amide proton resonance which in the first case arises from a direct effect, while in the second case, consistent with an earlier suggestion of Schwyzer and Ludescher, the deshielding would result from the extreme electronic lability of the peptide link which permits an electron density flow to the carbonyl. The solvent-induced chemical shift is shown to depend on the extent of exposure of the pertinent hydrogen and oxygen atoms so that the magnitude and direction of the effect reflect conformational features of the molecule at the amide sites. (auth)

Research Organization:
Univ. of California, Berkeley
OSTI ID:
7365395
Journal Information:
J. Am. Chem. Soc.; (United States), Vol. 97:16
Country of Publication:
United States
Language:
English