Total Chemical Synthesis of an Integral Membrane Enzyme: Diacylglycerol Kinase from Escherichia coli

被引：48

作者：

Lahiri, Sunanda ^{[3
]}

Brehs, Manuel ^{[1
,2
]}

Olschewski, Diana ^{[3
]}

Becker, Christian F. W. ^{[1
,2
]}

机构：

[1] Ctr Integrated Prot Sci, D-85747 Garching, Germany

[2] Tech Univ Munich, D-85747 Garching, Germany

[3] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 17期

关键词：

chemical protein synthesis; kinases; membrane proteins; native chemical ligation; protein folding; MECHANOSENSITIVE CHANNELS; SECONDARY STRUCTURE; DIGLYCERIDE KINASE; POTASSIUM CHANNEL; PROTEIN-SYNTHESIS; TERMINAL DOMAIN; H-RAS; OLIGOSACCHARIDES; SEMISYNTHESIS; BIOSYNTHESIS;

D O I：

10.1002/anie.201006686

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

From the ground up: Chemical synthesis provided direct access to a catalytically active membrane-embedded kinase with three transmembrane domains (TMs). Three key segments formed from the individual amino acids (represented by red and gray balls) by solid-phase peptide synthesis were connected by native chemical ligation (NCL; see picture); the synthetic protein underwent spontaneous folding in detergent micelles. ATP=adenosine 500triphosphate. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：3988 / 3992

页数：5

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