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Proton n.m.r. spectroscopic evidence for sulfur-aromatic interactions in peptides
International Journal of Peptide and Protein Research
|January 1, 1987
Abstract:
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.