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 …

Chemical protein modification has emerged as an invaluable tool for the development of
modified proteins. The complementary use of both genetic and chemical methods has …

Abstract Linear (Met1-linked) ubiquitination is involved inflammatory and innate immune
signaling. Previous studies have characterized enzymes regulating the addition and …

The modification of proteins with non‐protein entities is important for a wealth of
applications, and methods for chemically modifying proteins attract considerable attention …

Highlights•Dha in proteins is easily and flexibly accessible under mild conditions.•Dha
reactivity is used in β, γ-C–S/Se/N/C bond-formation and allows 'zero scar'protein …

The site-selective modification of peptide backbones allows an outstanding fine-tuning of
peptide conformation, folding ability, and physico-chemical and biological properties …

The reversible post‐translational modification of proteins by ubiquitin and ubiquitin‐like
proteins regulates almost all cellular processes, by affecting protein degradation …

α, β-Dehydroamino acids (dhAAs) are noncanonical amino acids that are found in a wide
array of natural products and can be easily installed into peptides and proteins. dhAAs …

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 …

Herein we introduce vinylphosphonothiolates as a new class of cysteine-selective
electrophiles for protein labeling and the formation of stable protein–protein conjugates. We …