Circular dichroism spectroscopy of folding in a protein monolayer

被引：14

作者：

Keegan, N

Wright, NG

Lakey, JH ^{[1
]}

机构：

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

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

[3] Newcastle Univ, Sch Elect Elect & Comp Engn, Inst Nanoscale Sci & Technol, Newcastle Upon Tyne NE1 7RU, Tyne & Wear, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 30期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

circular dichroism; monolayers; nanostructures; protein folding; surface plasmon resonance;

D O I：

10.1002/anie.200462977

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Thin but not invisible: The single layers of proteins needed for screening arrays and nanostructures can be studied by standard UV circular dichroism methods (see picture: colicin N P-domain on Au surface). In this way the conformational integrity of immobilized proteins can be measured under aqueous conditions, as is currently possible with their soluble counterparts. (Figure Presented) © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：4801 / 4804

页数：4

共 35 条

[1] A natively unfolded toxin domain uses its receptor as a folding template [J].