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Cysteine (symbol Cys or C; [5] / ˈ s ɪ s t ɪ iː n /) [6] is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine ...
Cysteine-rich proteins (CRP, cysteine-rich peptide or disulphide-rich peptide) are small proteins that contain a large number of cysteines. These cysteines either cross-link to form disulphide bonds , or bind metal ions by chelation , stabilising the protein's tertiary structure .
Rubicon (run domain Beclin-1-interacting and cysteine-rich domain-containing protein) is a protein that in humans is encoded by the RUBCN gene. [5] [6] Rubicon is one of the few known negative regulators of autophagy, a cellular process that degrades unnecessary or damaged cellular components. [7]
Cysteic acid also known as 3-sulfo-l-alanine is the organic compound with the formula HO 3 SCH 2 CH(NH 2)CO 2 H. It is often referred to as cysteate, which near neutral pH takes the form − O 3 SCH 2 CH(NH 3 +)CO 2 −. It is an amino acid generated by oxidation of cysteine, whereby a thiol group is fully oxidized to a sulfonic acid/sulfonate ...
Cysteine and glycine-rich protein 2 is a protein that in humans is encoded by the CSRP2 gene. [ 5 ] [ 6 ] [ 7 ] CSRP2 is a member of the CSRP family of genes, encoding a group of LIM domain proteins, which may be involved in regulatory processes important for development and cellular differentiation .
The C1 region contains one or two copies of a cysteine-rich domain, which is about 50 amino-acid residues long, and which is essential for DAG/PMA-binding. The DAG/PMA-binding domain binds two zinc ions; the ligands of these metal ions are probably the six cysteines and two histidines that are conserved in this domain.
CD163 (Cluster of Differentiation 163) is a protein that in humans is encoded by the CD163 gene. [5] CD163 is the high affinity scavenger receptor for the hemoglobin-haptoglobin complex [6] and in the absence of haptoglobin - with lower affinity - for hemoglobin alone. [7]
Selenocysteine has the same structure as cysteine, but with an atom of selenium taking the place of the usual sulfur. It has a selenol group. Like other natural proteinogenic amino acids, cysteine and selenocysteine have L chirality in the older D / L notation based on homology to D - and L-glyceraldehyde.