Disulfide bonds as switches for protein function.

  title={Disulfide bonds as switches for protein function.},
  author={Philip J Hogg},
  journal={Trends in biochemical sciences},
  volume={28 4},
The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs. The function of some secreted soluble proteins and cell-surface receptors is controlled by cleavage of one or more of their disulfide bonds; this cleavage is mediated by catalysts or facilitators that are specific for their substrate. 

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