Journal of Biochemistry Research

Oxydized Cysteine

Cysteine has a similar structure as serine, however with one of its oxygen iotas supplanted by sulfur; supplanting it with selenium gives selenocysteine. Like other regular proteinogenic amino acids, cysteine has l chirality in the more seasoned d/l documentation dependent on homology to d-and l-glyceraldehyde. In the more current R/S arrangement of assigning chirality, in view of the nuclear quantities of particles close to the hilter kilter carbon, cysteine (and selenocysteine) have R chirality, in light of the nearness of sulfur (or selenium) as a second neighbor to the unbalanced carbon. The remaining chiral amino acids, having lighter iotas in that position, have S chirality. The cysteine sulfhydryl bunch is nucleophilic and effectively oxidized. The reactivity is improved when the thiol is ionized, and cysteine buildups in proteins have pKa values near lack of bias, so are frequently in their responsive thiolate structure in the cell.

High Impact List of Articles

Relevant Topics in Medical