Examples of cysteine

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Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteins.
The disulfide bond that is normally formed by cysteine residues at positions 126 and 203 is indicated by a dashed line.
Since cystine signals were obtained from all peptides on both composition and sequence analyses, the two were considered to be cysteine residues.
The activities detected with all substrates used were decreased by treatment with cysteine proteinase inhibitors.
Cysteine proteinases from parasitic helminths have been recognized as important for parasite development and pathogenic damage to the hosts.
In the absence of cysteines and histidines, glutamate and aspartates can serve as sites of action.
The cysteine can then be exploited in two ways.
Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.
However, the short peptides did not encompass any sequence characteristic for functional domains of cysteine proteases.
Stage-specific requirement of cysteine during in vitro maturation of porcine oocytes for glutathione synthesis associated with male pronuclear formation.
These observations may explain the increasing attention addressed to cysteine proteases of parasites.
These conserved cysteines contribute to homodimer formation and function.
The 6 conserved cysteine residues are shaded in light grey.
The protein has a high disulphide content, 10% of all amino acid residues being disulphide-bonded cysteines.
It is also not suitable for proteins containing many cysteine residues.

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