Synthesis of post-translationally modified proteins

被引：10
|
作者：
van Kasteren, Sander [1 ]
机构：
[1] Netherlands Canc Inst NKI, Div Cell Biol 2, Biol Chem Lab, NL-1066 CX Amsterdam, Netherlands
来源：
BIOCHEMICAL SOCIETY TRANSACTIONS | 2012年 / 40卷
基金：
英国惠康基金;
关键词：
amber codon suppression; expressed protein ligation (EPL); modiform; native chemical ligation (NCL); post-translational modification (PTM); semi-synthesis; SITE-SPECIFIC INCORPORATION; UNNATURAL AMINO-ACIDS; GENETIC-CODE; TYROSINE PHOSPHORYLATION; ESCHERICHIA-COLI; CHEMICAL BIOLOGY; IN-VIVO; GLYCOPROTEIN-SYNTHESIS; RECOMBINANT PROTEINS; FIREFLY LUCIFERASE;
D O I：
10.1042/BST20120144
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Post-translational modifications of proteins can have dramatic effect on the function of proteins. Significant research effort has gone into understanding the effect of particular modifications on protein parameters. In the present paper, I review some of the recently developed tools for the synthesis of proteins modified with single post-translational modifications at specific sites in the protein, such as amber codon suppression technologies, tag and modify, and native chemical ligation.
引用
收藏
页码：929 / 944
页数：16
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