The 300 MHz nuclear magnetic resonance spectrum of the peptide hormone, oxytocin, in water, was obtained. Extensive nuclear magnetic resonance spindecoupling experiments, including those involving irradiation of the α proton resonances under the water peak, studies using partially deuterated hormone derivatives, and nuclear magnetic resonance studies of some precursor peptides to oxytocin, permitted us to assign most of the proton resonances of the hormone unambiguously. The J(Nα) values and temperature dependence of the chemical shift of the peptide amide and carboxamide protons of oxytocin were also obtained. These studies indicate that, in aqueous solution, oxytocin is a flexible molecule possessing several different conformations. Corresponding studies of [4 leucine] oxytocin were also made, with similar results and conclusions.
|Original language||English (US)|
|Number of pages||4|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|Issue number||12 (II)|
|State||Published - Jan 1 1973|
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