High-throughput screening of structural proteomics targets using NMR

被引：26

作者：

Galvao-Botton, LMP

Katsuyama, AM

Guzzo, CR

Almeida, FCL

Farah, CS

Valente, AP ^{[1
]}

机构：

[1] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05508900 Sao Paulo, Brazil

[2] Univ Fed Rio de Janeiro, Dept Bioquim Med, ICB, CCS, BR-21941590 Rio De Janeiro, Brazil

来源：

FEBS LETTERS | 2003年 / 552卷 / 2-3期

基金：

巴西圣保罗研究基金会;

关键词：

structural proteomics; NMR; X-ray; protein screening; target ORF; Xanthomonas citri;

D O I：

10.1016/S0014-5793(03)00926-8

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：

We applied a high-throughput strategy for the screening of targets for structural proteomics of Xanthoynonas axonopodis pv citri. This strategy is based on the rapid H-1-N-15 HSQC NMR analysis of bacterial lysates containing selectively 15N-labelled heterologous proteins. Our analysis permitted us to classify the 19 soluble candidates in terms of 'foldedness', that is, the extent to which they present a well-folded solution structure, as reflected by the quality of their NMR spectra. This classification allowed us to define a priority list to be used as a guide to select protein candidates for further structural studies. (C) 2003 Published by Elsevier B.V.

引用

页码：207 / 213

页数：7

共 39 条

[1] Selectively labeling the heterologous protein in Escherichia coli for NMR studies:: A strategy to speed up NMR spectroscopy [J].