Practical Protein Chemistry - A. Darbre 1989
Disulfide bonds
Identification and localization of cystine-containing peptides
General remarks
Assuming that the Amino Acid Sequence and the positions of most Disulfide Bonds in a protein have been established, it is obvious that the Location OF THE final disulfide bridge can be accepted without proof. For example, if the positions of three out of four bridges are determined unambiguously, it is reasonable to assume that the remaining bridge links the two unidentified half-cystine residues. As already noted, the Isolation of Cystine-containing Peptides can be accompanied by significant losses, with yields dropping below 50% in some cases. However, in the absence of contradictory evidence, even this is often quite sufficient for the unambiguous localization of S—S bridges. Naturally, this Conclusion holds true provided that the disulfide bonds remain stable within the protein molecule. A rare exception that is seldom encountered is ß-lactoglobulin [27], whose disulfide bonds are unstable.
Last update: 06/08/2026
Editorial and Educational Adaptation: This material has been compiled based on the primary/original source text. The project team performed an editorial review, corrected technical inaccuracies, structured sections, and adapted the content for an educational format.
What was processed:
- elimination of formatting defects (OCR errors, structural breaks, corrupted characters);
- editorial organization of content;
- standardization of terminology in accordance with academic sources;
- verification of factual statements against the original source text.
All mentions of the author, publication year, and origin of the primary text have been preserved in accordance with the source.