来自大肠杆菌核糖体蛋白S11中N-α-单甲基丙氨酸与赖氨酸之间的异肽键。
Isopeptide linkage between N-alpha-monomethylalanine and lysine in ribosomal protein S11 from Escherichia coli.
作者信息
Chen R, Chen-Schmeisser U
出版信息
Proc Natl Acad Sci U S A. 1977 Nov;74(11):4905-8. doi: 10.1073/pnas.74.11.4905.
Abstract
Protein S11 from the Escherichia coli ribosome has a unique NH2-terminal structure not previously observed among ribosomal proteins. Owing to the formation of an isopeptide bond between a secondary amino acid (N-alpha-monomethylalanine) and the epsilon-amino group of the NH2-terminal lysine residue, a "branching point" is formed. Therefore, two amino acids are seen when the NH2 terminus of the protein is determined.
摘要
来自大肠杆菌核糖体的蛋白质S11具有一种独特的NH2末端结构，这种结构在核糖体蛋白质中以前未曾观察到。由于在二级氨基酸（N-α-单甲基丙氨酸）和NH2末端赖氨酸残基的ε-氨基之间形成了异肽键，从而形成了一个“分支点”。因此，在确定该蛋白质的NH2末端时会看到两个氨基酸。
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