Proton n.m.r. spectroscopic evidence for sulfur-aromatic interactions in peptides.
The downfield shift of the tyrosyl proton resonances and an increased chemical shift difference between the resonances for the 2',6' and 3',5' hydrogens in a series of deamino-oxytocin analogs modified in the disulfide bridge provide evidence for aromatic-sulfur interactions in d6-dimethylsulfoxide solutions.
D004121:Dimethyl Sulfoxide; D004220:Disulfides; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009842:Oligopeptides; D013329:Structure-Activity Relationship; D013455:Sulfur; D014443:Tyrosine
D004220:Disulfides; D009842:Oligopeptides; D014443:Tyrosine; D013455:Sulfur; D004121:Dimethyl Sulfoxide