Probing protein function by chemical modification

被引：29

作者：

Wu, Yao-Wen ^{[1
,2
,3
]}

Goody, Roger S. ^{[1
]}

机构：

[1] Max Planck Inst Mol Physiol, Dept Phys Biochem, D-44227 Dortmund, Germany

[2] Kings Coll London, Div Cardiovasc, London SE1 1UL, England

[3] Kings Coll London, Randall Div Cell & Mol Biophys, London SE1 1UL, England

来源：

JOURNAL OF PEPTIDE SCIENCE | 2010年 / 16卷 / 10期

关键词：

protein labeling; fluorescent proteins; chemical probes; native chemical ligation; expressed protein ligation; protein trans-splicing; chemoselective reactions; bioorthogonal reactions; in vivo chemical labeling; Rab GTPases; prenylation; post-translational modification; CELL-SURFACE PROTEINS; SMALL-MOLECULE PROBES; TAG-FUSED PROTEIN; IN-VIVO; LIVING CELLS; RECOMBINANT PROTEINS; MAMMALIAN-CELLS; RHODIUM CARBENOIDS; PROTEOMIC ANALYSIS; SYNTHETIC PEPTIDE;

D O I：

10.1002/psc.1287

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：

Labeling proteins with synthetic probes, such as fluorophores, affinity tags, and other functional labels is enormously useful for characterizing protein function in vitro, in live cells, or in whole organisms. Recent advancements of chemical methods have substantially expanded the tools that are applicable to modify proteins. In this review, we discuss some important chemical methods for site-specific protein modification and highlight the application of established techniques to tackle biological questions. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.

引用

页码：514 / 523

页数：10

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