Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis
Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis
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DOI：
10.1016/s0969-2126(02)00894-8
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发表时间：
2002-12-01
期刊：
影响因子：
5.7
通讯作者：
Holak, TA
中科院分区：
文献类型：
--
作者：
Rehm, T;Huber, R;Holak, TA
在结构蛋白质组学时代，当蛋白质结构被定位在全基因组范围内时，检测出能够产生高质量核磁共振谱或X射线图像的表现良好的蛋白质是高通量结构确定的关键。简单的一维质子核磁共振谱已经为评估蛋白质的折叠性质提供了足够的信息。异核二维光谱通常用于揭示蛋白质的结构和结合性质的筛选。因此，核磁共振可以为优化适合于结构研究的蛋白质结构的条件提供重要信息。
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.