An approach to prepare membrane proteins for single-molecule imaging

被引：21

作者：

Cisneros, David A.

Muller, Daniel J.

Daud, Sofian M.

Lakey, Jeremy H. ^{[1
]}

机构：

[1] Newcastle Univ, Inst Cell & Mol Biosci, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

[2] Tech Univ Dresden, Biotechnol Zentrum, D-01307 Dresden, Germany

[3] Newcastle Univ, Inst Nanoscale Sci & Technol, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 20期

基金：

英国生物技术与生命科学研究理事会;

关键词：

lipids; membrane proteins; porin OmpF; protein structures; scanning force microscopy;

D O I：

10.1002/anie.200504506

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Observed from above: A cysteine mutation in a membrane protein enables it to be fixed in a defined orientation on flat gold surfaces (see picture, left). Subsequent coassembly with thiolipids produces clearly defined, immobilized proteins. Analysis by atomic force microscopy provides topographs of similar quality to those revealed from 2D crystals. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：3252 / 3256

页数：5

共 32 条

[1] MOLECULAR-LEVEL CONTROL OVER SURFACE ORDER IN SELF-ASSEMBLED MONOLAYER FILMS OF THIOLS ON GOLD [J].