Recently, self-healing polymers based on disulfide compounds have gained attention due to the versatile chemistry of disulfide bonds and easy implementation into polymeric materials. However, the underlying mechanisms of disulfide exchange which induce the self-healing effect in poly(disulfide)s remain unclear. In this work, we elucidate the process of disulfide exchange using a variety of spec...

The biogenesis of mitochondrial intermembrane space proteins depends on specific machinery that transfers disulfide bonds to precursor proteins. The machinery shares features with protein relays for disulfide bond formation in the bacterial periplasm and endoplasmic reticulum. A disulfide-generating enzyme/sulfhydryl oxidase oxidizes a disulfide carrier protein, which in turn transfers a disulf...

MOTIVATION Prediction of disulfide bond connectivity facilitates structural and functional annotation of proteins. Previous studies suggest that cysteines of a disulfide bond mutate in a correlated manner. RESULTS We developed a method that analyzes correlated mutation patterns in multiple sequence alignments in order to predict disulfide bond connectivity. Proteins with known experimental st...

The main function purpose of nanobiosensors is to sense a biologically specific material and the kind of sensing platform and doping engineering has been an emerging topic and plays an important role in monolayer molybdenum disulfide (mMoS2). In this paper, we theoretically reveal the electronic structures of mMoS2 doped by 3d transition metals. Furthermore, adsorption of nucleic acid [Adenine ...

8 3.1. Catalysis of oxidative protein folding 8 3.2 De novo formation of disulfide bonds in E. coli: the discovery of DsbA 9 3.3. DsbA is the most oxidizing disulfide catalyst 11 3.4. DsbB provides the periplasm with oxidizing power 15 3.5. Correcting wrong disulfide bonds in the periplasm: disulfide bond isomerization by DsbC 18 3.6. DsbD provides reducing equivalents in a highly oxidizing env...

The human pathogen Staphylococcus aureus does not utilize the glutathione thiol/disulfide redox system employed by eukaryotes and many bacteria. Instead, this organism produces CoA as its major low molecular weight thiol. We report the identification and purification of the disulfide reductase component of this thiol/disulfide redox system. Coenzyme A disulfide reductase (CoADR) catalyzes the s...

Introduction Human lactoferrin (hLF) is known to be a multifunctional protein of the transferrin family. It is a glycoprotein of approximately 80KDa and is present in various human secretory fluids including milk, saliva, tears and nasal secretions as well as being abundant in neutrophils [1-4]. The hLf protein includes 703 amino acids as a single polypeptide chain that folds into two similar g...

Although the structure of insulin has been well studied, the formation pathway of the three disulfide bridges during the refolding of insulin precursor is ambiguous. Here, we reported the in vitro disulfide-forming pathway of a recombinant porcine insulin precursor (PIP). In redox buffer containing L-arginine, the yield of native PIP from fully reduced/denatured PIP can reach 85%. The refolding...

The capacities to inhibit coumarin 7-hydroxylase activity of human cytochrome P450 2A6 (CYP2A6) by organosulfur compounds were evaluated. Five dialkyl sulfides and five dialkyl disulfides, with alkyl chains from methyl to amyl, were examined. In addition to these chemicals, diallyl sulfide, diallyl disulfide, allyl methyl sulfide, allyl n-propyl sulfide, allyl phenyl sulfide, diphenyl sulfide, ...

Increasing interest in production of protein-based pharmaceuticals (biotherapeutics) is accompanied by an increased need for verification of protein folding and correct disulfide bonding. Recombinant protein expression may produce aberrant disulfide bonds and could result in safety concerns or decreased efficacy. Thus, the thorough analysis of disulfide bonding is a necessity for protein therap...