disulfide bond


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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
References in periodicals archive ?
After RP-HPLC purification, mild oxidative conditions were employed to form the first A-chain intramolecular (A10-A15) disulfide bond, followed by a second purification.
The bacterial periplasm is an oxidizing environment that facilitates disulfide bond formation for correct protein folding and stability [9, 10].
Bacteria often do not form the correct disulfide bonds in recombinantly expressed proteins.
Here, the disulfide bonds within the cell, releasing the cargo inside the cell's cytosol within 15 to 30 min.
Molecular modeling studies have suggested four of these cysteines form two disulfide bonds necessary for furin function.
Tea amino acid residues from the N-terminus end of the 28 kDa protein showed 80 % homology with Excherichia coli thioredoxin, a protein that catalyzes reduction of a disulfide bond or oxidation of a thiol to a disulfide in cytoplasmic proteins.
Effects of disulfide bond reducing agents on sperm chromatin structural integrity and developmental competence of in vitro matured oocytes after intracytoplasmic sperm injection in pigs.
Herein, the disulfide bond has the high potential in not only reinforcing the durability during blood circulation but also enabling redox-sensitive release in the intracellular region.
Ruddock, "Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation," Antioxidants and Redox Signaling, vol.
This material was made by grafting the octadecyl methacrylate and disulfide bond to the PAM.
Sample CON 8% NPS Ionic bond (%) 1.14 [+ or -] 0.03 0.99 [+ or -] 0.02 Hydrogen bond (%) 1.79 [+ or -] 0.03 2.19 [+ or -] 0.02 Hydrophobic 47.84 [+ or -] 0.04 28.68 [+ or -] 0.00 interaction (%) Disulfide bond (%) 27.62 [+ or -] 0.07 12.27 [+ or -] 0.02 Sample 8% LMPS Ionic bond (%) 0.91 [+ or -] 0.01 Hydrogen bond (%) 2.93 [+ or -] 0.03 Hydrophobic 28.51 [+ or -] 0.05 interaction (%) Disulfide bond (%) 18.47 [+ or -] 0.06 CON (control, i.e., pure surimi gel), NPS (surimi gel with native potato starch), and LMPS (surimi gel with low-moisture potato starch).
A key feature of recent mechano-chemistry experiments at the single bond level is that the rate at which the reduction of a protein disulfide bond occurs in the presence of a nucleophile is exponentially dependent on the stretching force.