Interest in protein disulfide bond formation has recently increased because of the prominent
role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that …

If DNA is the information of life, then proteins are the machines of life—but they must be
assembled and correctly folded to function. A key step in the protein-folding pathway is the …

The recent growth in protein databases has revealed the functional diversity of many protein
superfamilies. We have assessed the functional variation of homologous enzyme …

A novel reagent, which introduces two sulfur atoms in one step, was designed and used for
the construction of diverse disulfanes by copper‐catalyzed oxidative cross‐coupling under …

Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible
NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an …

Several databases of protein structural families now exist—organised according to both
evolutionary relationships and common folding arrangements. Although these lag behind …

Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the
oxidation, reduction and isomerization of protein disulfides. In the endoplasmic reticulum …

The proteins from hyperthermophilic organisms maintain their biologically active structure at
temperatures that are significantly higher than the denaturation temperatures of their …

Disulfide, as a common structural motif, has been frequently used in pharmaceuticals, nature
products, and chemical biology. This chapter focuses on the methodologies that were …

An open reading frame optimized for expression of 6, 7-dimethyl-8-ribityllumazine synthase
of the hyperthermophilic bacterium Aquifex aeolicus in Escherichia coli was synthesized and …