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- W2043920377 abstract "The CD spectra of β-homoprolyl7-bradykinin (βHProB) and β-homophenylalanyl8-bradykinin (βHPheB) were compared to those of bradykinin. The spectra were analyzed in terms of models that have been proposed for the solution conformation of bradykinin. Cann et al. (1) proposed 3 → 1 hydrogen-bonding across Pro3, Pro7 and Phe8 in bradykinin, as shown by a 234 nm trough in the CD. The extra CH2 groups in the chains of the two bradykinin analogs would be expected to facilitate the proposed hydrogen-bonding, but in the case of βHProB the 234 nm trough is eliminated, and is reduced in magnitude for βHPheB. Ivanov et al. (2) proposed a cyclic conformation for bradykinin, stabilized by ionic attraction between the side-chain of Arg1 and the carboxylate terminal. The extra CH2 groups of these two analogs would be expected to increase the stability of such a conformation, and there was some evidence that the ionic effects on the CD spectra of the two analogs were different from those on the bradykinin spectra. Alternatively, the effects could be attributed to cis-trans isomerizations around the prolyl peptide bonds." @default.
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- W2043920377 date "1977-04-01" @default.
- W2043920377 modified "2023-09-25" @default.
- W2043920377 title "Circular dichroism spectra of bradykinin analogs containing β-homoamino acids" @default.
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- W2043920377 doi "https://doi.org/10.1016/0006-291x(77)91537-6" @default.
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