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 …

Publisher Summary This chapter summarizes the experimental information on protein
energetics. This field is develo** fast and the concept of the energetics of protein structure …

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 …

Significance: Disulfides are important building blocks in the secondary and tertiary structures
of proteins, serving as inter-and intra-subunit cross links. Disulfides are also the major …

Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

Publisher Summary Disulfide-bond formation is a versatile oxidation used biologically in
diverse processes, such as enzyme catalysis, protection against oxidative damage …

Protein disulphide isomerase (PDI) has been known for many years to assist in the folding of
proteins containing disulphide bonds, but the exact mechanism by which it achieves this is …

▪ Abstract Disulfide bonds formed between pairs of cysteines are important features of the
structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia …

The enzymes of the protein disulfide isomerase (PDI) family are thiol–disulfide
oxidoreductases of the endoplasmic reticulum (ER). They contain a CXXC active-site …

Glutaredoxins belong to the thioredoxin superfamily of structurally similar thiol-disulfide
oxidoreductases catalyzing thiol-disulfide exchange reactions via reversible oxidation of two …