Practical Protein Chemistry - A. Darbre 1989

Chemical Fragmentation of Polypeptides
Conclusion

Currently, A number of chemical Methods for Peptide bond Cleavage at specific amino acid residues are known. The practical applicability of a reagent or method is determined primarily by the Specificity and completeness of the reaction. This chapter discusses in detail those methods that have found, and are likely to continue to find, Structure/182.html">Practical Application precisely because they best satisfy these two requirements.

Due to its high specificity and near-quantitative product yield, Cyanogen bromide Cleavage at Methionine Residues is widely used in Protein Chemistry. Satisfactory methods for cleaving peptide bonds at Tryptophan and Cysteine have also been developed and proven in practice.

At the same time, no single method provides an ideal set of fragments sufficient for reconstructing the complete Amino Acid Sequence. Achieving this goal requires an optimal combination of chemical and enzymatic methods. Chemical methods of peptide bond cleavage find application in peptide chemistry. Chemical modification methods can also be employed in the synthesis of biologically active Peptides via Recombinant DNA technology.

Following the discovery that neighboring group effects, such as 1,5-interactions, are the primary cause of peptide bond cleavage in $\gamma$-substituted Amino Acids—specifically $\gamma,\delta$-dihydroxyleucine in phalloidin [204]—this principle was extended to The Study of peptides composed of Other Amino Acids. Throughout The Development of protein structural analysis methods, numerous Reagents have been investigated, yet many still await evaluation and may eventually expand the researcher's toolkit.