Roder H, Elöve G A, Englander S W
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.
Nature. 1988 Oct 20;335(6192):700-4. doi: 10.1038/335700a0.
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 cytochrome c show 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.
为了理解蛋白质折叠的过程,有必要获取有关折叠中间体的详细结构信息。目前正在通过氢交换和快速混合来标记瞬态结构中间体,并随后利用二维核磁共振波谱分析质子标记模式,以此研究这个难题。细胞色素c的研究结果表明,该方法提供了必要的空间和时间分辨率,能够在从毫秒到分钟的时间尺度上,监测多肽链上许多特定位点的结构形成。