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Protein Cysteine | Open Access Journals
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Journal of Bioprocessing & Biotechniques

ISSN: 2155-9821

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Protein Cysteine

Protein cysteine is traditionally considered a hydrophilic aminoalkanoic acid , based largely on the chemical parallel between its sulfhydryl group and therefore the hydroxyl groups within the side chains of other polar amino acids. However, the side chain of cysteine has been shown to stabilize hydrophobic interactions in micelles to a greater degree than the side chain in non-polar aminoalkanoic acid glycine and polar aminoalkanoic acid serine. during a statistical analysis of the frequency with which amino acids appear in several chemical environments in protein structures, free cysteine residues were found to accompany the hydrophobic regions of proteins. Their hydrophobic tendency was like that of known non-polar amino acids like methionine and tyrosine (tyrosine is aromatic polar but also hydrophobic), of which those were far more important than those of known polar amino acids like serine and threonine. Hydrophobicity scales, which classify amino acids from the foremost hydrophobic to the foremost hydrophilic, systematically place cysteine towards the hydrophobic end of the spectrum, even once they are supported methods which aren't influenced by the tendency of cysteines to make disulfide bonds in proteins. Besides its oxidation to cystine, cysteine participates in many post-translational modifications. The nucleophilic sulfhydryl group allows cysteine to conjugate with other groups, for instance in prenylation. Ubiquitin ligase transfers ubiquitin to its counterpart, its proteins and its caspases, which engage in proteolysis within the apoptotic cycle. The intines often function with the assistance of a catalytic cysteine. These roles are generally limited to the intracellular environment, where the environment is reduced, and therefore the cysteine isn't oxidized to cystine.

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