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The structure of a disulfide bond can be described by its χ ss dihedral angle between the C β −S γ −S γ −C β atoms, which is usually close to ±90°. The disulfide bond stabilizes the folded form of a protein in several ways: It holds two portions of the protein together, biasing the protein towards the folded topology.
Although the first phosphorus compounds observed to act as cholinesterase inhibitors were organophosphates, [90] the vast majority of nerve agents are instead phosphonates containing a P-C bond. Only a handful of organophosphate nerve agents were developed between the 1930s and 1960s, including diisopropylfluorophosphate , VG and NPF .
The dithiophosphine ylides are normally attacked at the phosphorus atom by a nucleophile, for instance the reaction of an alkoxide, phenolate, alcohol or phenol with a 1,3,2,4-dithiadiphosphetane 2,4-disulfide can form a new compound with a phosphorus-oxygen bond.
By transferring the disulfide bond between these two cysteine residues onto the folding protein it is responsible for the latter's oxidation. In contrast to bacteria, where the oxidative and isomerization pathways are carried out by different proteins, PDI is also responsible for the reduction and isomerization of the disulfide bonds.
In industrial and environmental chemistry, an organophosphorus compound need contain only an organic substituent, but need not have a direct phosphorus-carbon (P-C) bond. [citation needed] Thus a large proportion of pesticides (e.g., malathion), are often included in this class of compounds.
Since orthophosphoric acid has three −OH groups, it can esterify with one, two, or three alcohol molecules to form a mono-, di-, or triester. See the general structure image of an ortho- (or mono-) phosphate ester below on the left, where any of the R groups can be a hydrogen or an organic radical. Di- and tripoly- (or tri-) phosphate esters ...
DsbC and DsbG facilitate the proper folding of the protein by breaking non-native disulfide bonds. In addition to this, DsbC also shows chaperone activity. [1] [3] The reduced cysteine on DsbC performs a nucleophilic attack on the target non-native disulfide bond, to form an unstable disulfide bond between DsbC and the protein. Another thiolate ...
In biochemistry, dephosphorylation is the removal of a phosphate (PO 3− 4) group from an organic compound by hydrolysis. It is a reversible post-translational modification . Dephosphorylation and its counterpart, phosphorylation , activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides .