Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

During the maturation of extracellular proteins, disulfide bonds that chemically cross-link
specific cysteines are often added to stabilize a protein or to join it covalently to other …

Sulfur and selenium occur in proteins as constituents of the amino acids cysteine,
methionine, selenocysteine, and selenomethionine. Recent research underscores that these …

Highlights•The need for recombinant proteins both as biopharmaceuticals and for structural
studies in drug development is outlined.•The basis of the production of recombinant proteins …

In biological systems, the amino acid cysteine combines catalytic activity with an extensive
redox chemistry and unique metal binding properties. The interdependency of these three …

Mycobacteria have low-permeability outer membranes that render them resistant to most
antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins …

We describe here a pathway for the import of proteins into the intermembrane space (IMS) of
mitochondria. Substrates of this pathway are proteins with conserved cysteine motifs, which …

The F sex factor of Escherichia coli is a paradigm for bacterial conjugation and its transfer
(tra) region represents a subset of the type IV secretion system (T4SS) family. The F tra …

Cys is much different from other common amino acids in proteins. Being one of the least
abundant residues, Cys is often observed in functional sites in proteins. This residue is …

Transcriptional profiles of Pseudomonas aeruginosa exposed to two separate copper stress
conditions were determined. Actively growing bacteria subjected to a pulse of elevated …