作者: Bryan Schmidt , Lorraine Ho , Philip J. Hogg
DOI: 10.1021/BI0603064
关键词:
摘要: Protein disulfide bonds link cysteine residues in the polypeptide chain. The contribute, sometimes crucially, to protein stability and function are strongly conserved through evolution of species. By analyzing conservation all structurally validated across 29 completely sequenced eukaryotic genomes, we found that disulfide-bonded cysteines even more than tryptophan – most amino acid. Moreover, rate acquisition shows a strong positive correlation with organism complexity, which probably reflects requirement for sophistication complex majority perform structural role by stabilizing mature protein. Some functional can be divided into catalytic or allosteric disulfides. Catalytic disulfides/dithiols transfer electrons between proteins, while control they reside when break and/or form. There currently dozen so examples bonds. features these their involvement respective proteins’ discussed. A common aspect 11 12 discussed herein is β-strands β-loops.