Examples of disulfide

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The disulfide crosslinking experiment does not prove that the crystal structure of the hammerhead ribozyme is the catalytically active structure.
The reduction of a disulfide is a two-electron process while ferredoxin is a one-electron carrier.
Overcoming residual frustration in domain-swapping: the roles of disulfide bonds in dimerization and aggregation.
Both ribozymes were active within a factor of two of wild-type activity when the disulfide bond was reduced.
Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.
The disulfide bond that is normally formed by cysteine residues at positions 126 and 203 is indicated by a dashed line.
Upon reduction of the disulfide by thioredoxin, the insertion is destabilized, as seen in the spinach structure, and the strands are released.
There is a stretch of 11 residues separating the two cysteines involved in the disulfide.
In this step, one electron from the ferredoxin and one electron from the iron-sulfur cluster are used to cleave the disulfide bridge.
The structure of the enzyme was recently determined and provides the framework for this reduction revealing close contacts between the iron-sulfur center and the disulfide.
This is an indication that the endopeptidase has peptide chains connected by disulfide bridges.
These disulfide bridges are primary contributors to the 3-dimensional structure of the protein, as there is limited secondary structure.
However, as they note, no such cysteine-sulfide disulfide has been observed previously.
In each of the extensions is one regulatory disulfide bridge present.
An intact interchain disulfide bond is required for the neurotoxicity of tetanus toxin.

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