Abstract
Abstract NMR spectroscopy is a versatile method for the conformational analysis of peptides and proteins. The hydrogen–chlorine exchange of amide NH protons is detected by 1H NMR and used as a method to distinguish between intramolecularly hydrogen-bonded and solvent-exposed NH moieties. The method has been applied to hydrogen bond detection in naturally occurring antibiotic peptides, such as gramicidin S, and CH3CONH–X (X = alkyl- or aryl-) derivatives. The deuterium exchange method was compared with this method in parallel experiments. In the case of chlorine exchange, in contrast to deuterium exchange, the hydrogen-bonded amide protons are replaced much faster than their solvent-exposed counterparts and the duration of the experiments is considerably less. It is highly possible that the hydrogen–chlorine exchange reaction under the present experimental conditions, in the dark and at room temperature, proceeds through an electrophilic polar mechanism.
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