Total chemical synthesis and X-ray crystal structure of a protein diastereomer: [D-Gln 35]ubiquitin

被引：81

作者：

Bang, D

Makhatadze, GI

Tereshko, V

Kossiakoff, AA

Kent, SB ^{[1
]}

机构：

[1] Univ Chicago, Inst Biophys Dynam, Chicago, IL 60637 USA

[2] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA

[3] Univ Chicago, Dept Chem, Chicago, IL 60637 USA

[4] Penn State Univ, Dept Biochem & Mol Biol, Hershey, PA 17033 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 25期

关键词：

chemical ligation; diastereomers; protein structures; protein synthesis; X-ray diffraction;

D O I：

10.1002/anie.200463040

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Striking similarity: An efficient synthetic route to native ubiquitin and its diastereomer [D-Gln35]ubiquitin was realized by combining a one-pot native chemical ligation process with protein desulfurization. High-resolution X-ray crystallographic studies of the protein diastereomer (see picture) revealed a striking conservation of molecular structure. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：3852 / 3856

页数：5

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