Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis

被引：68

作者：

Rehm, T ^{[1
]}

Huber, R ^{[1
]}

Holak, TA ^{[1
]}

机构：

[1] Max Planck Inst Biochem, D-82152 Munich, Germany

来源：

STRUCTURE | 2002年 / 10卷 / 12期

关键词：

NMR; X-ray crystallography; screening; protein characterization; proteomics; structural analysis;

D O I：

10.1016/S0969-2126(02)00894-8

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：

In the time of structural proteomics when protein structures are targeted on a genome-wide scale, the detection of "well-behaved" proteins that would yield good quality NMR spectra or X-ray images is the key to high-throughput structure determination. Already, simple one-dimensional proton NMR spectra provide enough information for assessing the folding properties of proteins. Heteronuclear two-dimensional spectra are routinely used for screenings that reveal structural, as well as binding, properties of proteins. NMR can thus provide important information for optimizing conditions for protein constructs that are amenable to structural studies.

引用

页码：1613 / 1618

页数：6

共 26 条

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