Abstract Disulfide-bond formation between the side chains of cysteine–cysteine pairs is often critical to the folding behavior, stability, and functionality of proteins. In this paper, we report that sulfur atoms can be introduced into the amide groups of aminoxy peptides to form a novel type of disulfide bridge, which creates a connecting loop in the peptide backbone.
[Johnson, James E.; Ghafouripour, Abdolkarim; Kunz Haug, Yvonne; Cordes, A. Wallace; Pennington, William T.; Exner, Otto Journal of Organic Chemistry, 1985 , vol. 50, # 7 p. 993 - 997]
[Johnson, James E.; Ghafouripour, Abdolkarim; Kunz Haug, Yvonne; Cordes, A. Wallace; Pennington, William T.; Exner, Otto Journal of Organic Chemistry, 1985 , vol. 50, # 7 p. 993 - 997]
