How to study proteins by circular dichroism

被引：2620

作者：

Kelly, SM ^{[1
]}

Jess, TJ ^{[1
]}

Price, NC ^{[1
]}

机构：

[1] Univ Glasgow, Inst Biomed & Life Sci, Div Biochem & Mol Biol, Glasgow G12 8QQ, Lanark, Scotland

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2005年 / 1751卷 / 02期

基金：

英国生物技术与生命科学研究理事会;

关键词：

circular dichroism; protein structure; secondary structure; protein folding; ligand binding;

D O I：

10.1016/j.bbapap.2005.06.005

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：

Circular dichroism (CD) is being increasingly recognised as a valuable technique for examining the structure of proteins in solution. However, the value of many studies using CD is compromised either by inappropriate experimental design or by lack of attention to key aspects of instrument calibration or sample characterisation. In this article, we summarise the basis of the CD approach and its application to the study of proteins, and then present clear guidelines on how reliable data can be obtained and analysed. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：119 / 139

页数：21

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