The ability to manipulate the chemical composition of proteins and peptides has been
central to the development of improved polypeptide-based therapeutics and has enabled …

Inteins are nature's escape artists; they facilitate their excision from flanking polypeptides
(exteins) concomitant with extein ligation to produce a mature host protein. Splicing requires …

Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an
encyclopedic work describing the many approaches to the site-specific modification of …

Inteins catalyze a post-translational modification known as protein splicing, where the intein
removes itself from a precursor protein and concomitantly ligates the flanking protein …

Protein splicing is a posttranslational modification where intervening proteins (inteins)
cleave themselves from larger precursor proteins and ligate their flanking polypeptides …

Inteins are mobile genetic elements that apply standard enzymatic strategies to excise
themselves post-translationally from the precursor protein via protein splicing. Since their …

The p K a values of a series of chiral Brønsted acids, including N-triflylphosphoramides, bis
(sulfonyl) imides, bis (sulfuryl) imides, dicarboxylic acids, sulfonic acids, and N-phosphinyl …

Intein enzymes catalyze the splicing of their flanking polypeptide chains and have found
tremendous biotechnological applications. Their terminal residues form the catalytic core …

Inteins are mobile genetic elements that self-splice at the protein level. Mycobacteria have
inteins inserted into several important genes, including those corresponding to the iron …

In a protein, nearby titratable sites can be coupled: the (de) protonation of one may affect the
other. The degree of this interaction depends on several factors and can influence the …