A disulfide bond
or a peptide linker is engineered to link the heavy and light chain of the antibodies to form a single-chain variable fragment (scFv) or disulfide-stabilized scFv (scdsFv).
The essential principle of the Erel and Neselioglu method is the reduction of disulfide bonds
(S=S) to reactive thiol groups in the presence of NaB[H.
At the same time, it can enhance disulfide bond
formation in the cytosolic fraction due to mutations of trxB and gor genes.
Hogg, "Post-translational control of protein function by disulfide bond
cleavage," Antioxidants and Redox Signaling, vol.
Another approach for intrinsic self-healing is by means of the formation of covalent bonds that allow chain exchange reactions such as the dynamic reversible formation of acylhydrazones , trithiocarbonates reshuffling , the reaction exchange of siloxane segments [13, 14], and the metathesis reaction of disulfide bonds
A proposed working model states that reduced PDI, secreted by activated platelets, reacts with low procoagulant activity TF to yield a TF with high procoagulant activity through the formation of a disulfide bond
2]S induces angiogenesis mediated by vascular endothelial growth factor receptor 2 (134), (135) by reducing a disulfide bond
located between cysteine 1045 and cysteine 1024.
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.
Effects of disulfide bond
formation on N-linked glycosylation and secretion.
coli, those on protein folding and quality control include disulfide bond
formation in the periplasm, those on practical implications include protein accumulation and expression of antibody fragments and an article examines methods for the computational prediction of periplasmic proteins.
Curlaway is able to do both, because it is nonalkaline and does not break the disulfide bond
; it relaxes gradually and gently by rotating only the anchors of the disulfide bond
in the hair matrix.
A posttranslational cleavage by host-derived enzymes generates 2 polypeptides that remain linked by a disulfide bond
Iodoacetamide Tagging of Critical Cysteine Residues Within the Catalytic Domain of Furin Provides Evidence of Disulfide Bond
Gilliland, The Crystal Structure of the Disulfide-stabilized Fv Fragment of Anticancer Antibody B1: Conformational Influence of an Engineered Disulfide Bond
, Proteins 31(2), 128-138 (1998).