Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics

被引：112

作者：

Wallace, BA ^{[1
]}

Janes, RW

机构：

[1] Univ London Birkbeck Coll, Sch Crystallog, London WC1E 7HX, England

[2] SERC, Daresbury Lab, Ctr Prot & Membrane Struct & Dynam, Warrington WA4 4AD, Cheshire, England

[3] Univ London Queen Mary & Westfield Coll, Sch Biol Sci, London E1 4NS, England

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2001年 / 5卷 / 05期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/S1367-5931(00)00243-X

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：

Recent developments in instrumentation and bioinformatics show that the technique of synchrotron radiation circular dichroism spectroscopy can provide novel information on protein secondary structures and folding motifs, and has the potential to play an important role in structural genomics studies, both as a means of target selection and as a high-throughput, low-sample-requiring screening method. This is possible because of the additional information content in the low-vacuum ultraviolet wavelength data obtainable with intense synchrotron radiation light sources, compared with that present in spectra from conventional lab-based circular dichroism instruments.

引用

页码：567 / 571

页数：5

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