STRUCTURAL CHARACTERIZATION OF FOLDING INTERMEDIATES IN CYTOCHROME-C BY H-EXCHANGE LABELING AND PROTON NMR
STRUCTURAL CHARACTERIZATION OF FOLDING INTERMEDIATES IN CYTOCHROME-C BY H-EXCHANGE LABELING AND PROTON NMR
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DOI：
10.1038/335700a0
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发表时间：
1988-10-20
期刊：
影响因子：
64.8
通讯作者：
ENGLANDER, SW
中科院分区：
文献类型：
--
作者：
RODER, H;ELOVE, GA;ENGLANDER, SW
为了了解蛋白质折叠的过程，有必要获得折叠中间体的详细结构信息。正在通过使用氢交换和快速混合来标记瞬态结构中间体来研究这个难题，随后通过二维核磁共振波谱分析质子标记模式。细胞色素c的结果表明，该方法提供了在毫秒到分钟的时间尺度上监测多肽链上许多定义位点的结构形成所需的空间和时间分辨率。
To understand the process of protein folding, it will be necessary to obtain detailed structural information on folding intermediates. This difficult problem is being studied by using hydrogen exchange and rapid mixing to label transient structural intermediates, with subsequent analysis of the proton-labelling pattern by two-dimensional nuclear magnetic resonance spectroscopy. Results for cytochromecshow that the method provides the spatial and temporal resolution necessary to monitor structure formation at many defined sites along the polypeptide chain on a timescale ranging from milliseconds to minutes.