Cysteine: Difference between revisions
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Cysteine (abbreviated to Cys or C) is an amino acid with the side chain -CH<sub>2</sub>SH. Cysteine, like [[Methionine|methionine]], contains sulphur. It is a non-polar [[Amino acids|amino acid that]] contains a very reactive thiol or [[ | Cysteine (abbreviated to Cys or C) is an [[Amino_acid|amino acid]] with the side chain -CH<sub>2</sub>SH. Cysteine, like [[Methionine|methionine]], contains [[Sulphur|sulphur]]. It is a non-polar [[Amino acids|amino acid that]] contains a very reactive thiol or [[Sulfhydryl group|sulfhydryl group]] (-SH). The presence of this group allows cysteine to form strong [[Disulphide bridges|disulphide bridges]] when paired with another cysteine. Cysteine therfore plays an important structural role in [[Proteins|proteins]]. The ability of cysteine to form [[Disulphide_bridges|disulphide bridges]] is of great significance for [[Proteins|proteins]] that have to work outside of the [[Cell|cell]]. This is because the cysteine side chain of these [[Protein|proteins]] forms [[Disulphide_bond|disulphide bonds]] which increases the stability of the [[Proteins|proteins]]. However, it should be noted that [[Proteins|proteins]] working inside the cell do not form [[Disulphide_bond|disulphide bonds]] <ref>Berg et al., Biochemistry, 6th Edition, 2007: 31.</ref>. <br> | ||
=== '''References''' === | === '''References''' === | ||
<references /> | <references /> | ||
Revision as of 15:07, 23 October 2012
Cysteine (abbreviated to Cys or C) is an amino acid with the side chain -CH2SH. Cysteine, like methionine, contains sulphur. It is a non-polar amino acid that contains a very reactive thiol or sulfhydryl group (-SH). The presence of this group allows cysteine to form strong disulphide bridges when paired with another cysteine. Cysteine therfore plays an important structural role in proteins. The ability of cysteine to form disulphide bridges is of great significance for proteins that have to work outside of the cell. This is because the cysteine side chain of these proteins forms disulphide bonds which increases the stability of the proteins. However, it should be noted that proteins working inside the cell do not form disulphide bonds [1].
References
- ↑ Berg et al., Biochemistry, 6th Edition, 2007: 31.