Protein phosphorylation is a crucial regulator of protein and cellular function, yet, despite
identifying an enormous number of phosphorylation sites, the role of most is still unclear …

The native chemical ligation reaction (NCL) involves reacting a C-terminal peptide thioester
with an N-terminal cysteinyl peptide to produce a native peptide bond between the two …

The present review offers an overview of nonclassical (eg, with no pre-or in situ activation of
a carboxylic acid partner) approaches for the construction of amide bonds. The review aims …

Peptide thioesters play a key role in convergent protein synthesis strategies such as native
chemical ligation, traceless Staudinger ligation, and Ag+‐mediated thioester ligation. The …

Intramolecular ligation of peptide hydrazides is reported to occur readily, causing the
lactamization of fully unprotected peptides in an epimerization-free manner. This method …

With two β-mercaptoethyl groups on the N, a tertiary amide of structure 1 is always poised for
intramolecular thioesterification however it flips about the C− N bond. It is shown that a …

N→ S acyl-transfer-mediated synthesis of peptide thioesters utilizing an N-aminoacyl-N-
sulfanylethylaminobenzoic acid derivative has been examined. The developed synthetic …

An operationally simple method for the synthesis of peptide thioesters is developed using
standard Fmoc solid-phase peptide synthesis procedures. The method relies on the use of a …

The size of information that can be stored in nucleic acids, proteins, and carbohydrates was
calculated. The number of hexamers for peptides is 64,000,000 (20 6) and seems to be …

The native chemical ligation enables the chemoselective coupling of two unprotected
protein segments. In the initial format of this reaction, the side chain of N‐terminal cysteine …