disulfide bond


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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
References in periodicals archive ?
TG2 is now also the first protein known to have a reversible disulfide bond on/off switch of this type.
After binding to the specific receptor, internalization of PE occurs through clathrin-coated pits into the endocytic compartment, and then PE is proteolytically cleaved in between amino acid (AA) 270 and 280, with the reduction of the disulfide bond connecting residues 265 and 287, which results in a fragment of 37,000 (AA280-612) at the C-terminus.
Thiols engage in oxidation reactions with oxidant molecules, forming disulfide bonds.
coli since contains multiple disulfide bonds and reductive environment of cytoplasm does not let correct disulfide bond formation resulting in generally misfolded and biologically-inactive inclusion bodies (2,24).
2]GPI is around Cys288-Cys326 disulfide bond and the redox state of this could affect cellular immune processes mediated by [[beta].
The TBP can nucleophilically attack one of the sulfur atoms of the disulfide bond to form transient species with phosphonium and thioxides groups.
In platelets, PDI is known for its paramount importance in platelet aggregation through the isomerization of a disulfide bond in the [[alpha].
2]S activates NMDA receptors by reducing the cysteine disulfide bond.
The C8[alpha] MACPF sequence is distinctive in that it contains a unique indel (insertion/deletion) between residues 159-175, which includes C164 that forms the disulfide bond to C40 in C8[gamma].
DISULFIND server shows that the position of six cysteine peptides of gambicin could not favour disulfide bond formation and shows less stable structure.
The active toxic A-chain is covalently linked via a disulfide bond to the sugar binding B-chain, this bond being biologically important as the individual chains are biologically inactive.
The disulfide bond is sandwiched between a pyrene section on one side and a biotin section on the other.