disulfide bond

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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
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A previous study also showed that conserved disulfide bridges in avian-[beta]-defensin-12 are essential for the chemotactic property and maximum antimicrobial activity [27].
Thiols, which include a sulfhydryl (-SH) group, constitute one of the defense systems against unfavorable effects of ROS, and are the main target of ROS, being oxidized by oxidant molecules to form reversible disulfide bridges. These formed disulfide bridges may be reduced to thiol groups.
These cysteine residues fold the mature peptide through disulfide bridges in all decapod families (Ventura et al., 2014).
She said, 'It helps in stiffening of outer dense fibers by formation of disulfide bridges or strong bonding protein molecules during sperm maturation, which is an essential step for generation of sperm motility, especially progressive motility as shown in the study.' Zinc deficiency affects sperm production, maturation and motility, as well as fertilizing capacity of the active matured sperm cells, the study said.
The extent of crosslinking was expected to be a primary parameter governing stability of the base polymer layer; moreover, by deactivating PMPMS thiols it serves to prevent their subsequent participation in immobilization of thiolcarrying biomolecules through alternate pathways such as formation of disulfide bridges [37].
Under reducing conditions, disulfide bridges in proteins are disrupted, whereas such interactions are preserved under nonreducing conditions.
In the article "Efficient Self-Assembly of mPEG End-Capped Porous Silica as a Redox-Sensitive Nanocarrier for Controlled Doxorubicin Delivery," porous nanosilica particles are modified with PEG shell via disulfide bridges and supramolecular interaction for drug delivery, with benefits of enhanced drug loading capacity and decreased risk of systemic toxicity.
For example, the formation of disulfide bridges within the peptide will create 'protein folding' containing the carbon-14 label.
(2015) Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity.
The following disulfide bridges were identified: intrachain [Cys(L23)-Cys(L88), Cys(L134) Cys(L194), Cys(H22)-Cys(H96), Cys (H146)-Cys(H202), Cys(H263)-Cys(H323), Cys(H369)-Cys(H427)] and interchain [Cys(L214)-Cys(H222), Cys(H228)-Cys(H228), Cys(H231)-Cys(H231)].
The mutagenesis data allowed for concluding that the presence of disulfide bridges is not required for folding of the Na,K-ATPase [alpha]-subunit and its subsequent activity [24].
The first class contains 60-70 amino acids cross linked by four disulfide bridges (Gordon et al., 2003).