The oxidative folding of the Amaranthus α-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the intermediate ...

IscS and IscU from Escherichia coli cooperate with each other in the biosynthesis of iron-sulfur clusters. IscS catalyzes the desulfurization of L-cysteine to produce L-alanine and sulfur. Cys-328 of ...

As the most reactive member of nature’s standard stable of amino acids, cysteine is commonly tapped as a nucleophile in enzyme active sites. But cysteine’s reactivity also makes it uniquely ...

Certain types of peptides and microproteins for drug discovery research can be made more efficiently and quickly using a reaction solvent that helps mimic nature's way Cysteine is one of the many ...

Make room, disulfide crosslinks. There’s a new kind of crosslink in proteins. Instead of an S–S bridge connecting two cysteine residues, it consists of an N–O–S bridge between a lysine and a cysteine.

This research proposal presents a comprehensive investigation into the structural and functional integrity of disulfide bonds within therapeutic proteins, emphasizing their critical role in ...

Mutations in copper-zinc superoxide dismutase 1 (SOD1) derail folding of the protein, preventing it from playing nice with its siblings. This leads the mutant down a path to aggregation and ...

A new wave of antibody-targeted anticancer therapies is showing great clinical promise, with the potential to transform cancer treatment. These antibody-drug conjugates (ADCs) are multicomponent ...