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 …

Peroxynitrite is a short-lived and reactive biological oxidant formed from the diffusion-
controlled reaction of the free radicals superoxide (O2•–) and nitric oxide (• NO). In this …

Current methods used for measuring amino acid side-chain reactivity lack the throughput
needed to screen large chemical libraries for interactions across the proteome. Here we …

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

The clinical and commercial success of covalent drugs has prompted a renewed and more
deliberate pursuit of covalent and irreversible mechanisms within drug discovery. A covalent …

Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is
tuned to perform diverse biochemical functions. The absence of a consensus sequence that …

Zinc and cellular oxidants such as reactive oxygen species (ROS) each participate in a
multitude of physiological functions. There is considerable overlap between the affected …

Background Disulfide bond formation is a key posttranslational modification, with
implications for structure, function and stability of numerous proteins. While disulfide bond …

Cysteine thiols are among the most reactive functional groups in proteins, and their pairing
in disulfide linkages is a common post-translational modification in proteins entering the …

Zinc fingers (ZFs) are among the most structurally diverse protein domains. They interact
with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes …