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 …

Protecting group chemistry for the cysteine thiol group has enabled a vast array of peptide
and protein chemistry over the last several decades. Increasingly sophisticated strategies for …

Methods to prepare proteins that include a specific modification at a desired position are
essential for understanding their cellular functions and physical properties in living systems …

The addition of O-linked-β-DN-acetylglucosamine (O-GlcNAc) onto serine and threonine
residues of nuclear and cytoplasmic proteins is an abundant, unique post-translational …

The field of site‐specific modification of proteins has drawn significant attention in recent
years owing to its importance in various research areas such as the development of novel …

The acetamidomethyl (Acm) moiety is a widely used cysteine protecting group for the
chemical synthesis and semisynthesis of peptide and proteins. However, its removal is not …

Organic chemistry allows for the modification and chemical preparation of protein analogues
for various studies. The thiolate side chain of the Cys residue has been a key functionality in …

Histone ubiquitination affects the structure and function of nucleosomes through tightly
regulated dynamic reversible processes. The efficient preparation of ubiquitinated histones …

Chemical synthesis is a well‐established method for the preparation in the research
laboratory of multiple‐tens‐of‐milligram amounts of correctly folded, high purity protein …

Conspectus Chemical protein synthesis has been proved as an efficient way to afford
medium-sized proteins with high homogeneity in workable quantities for various …