Functional dynamics of proteins revealed by solution NMR
Functional dynamics of proteins revealed by solution NMR
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DOI：
10.1016/j.sbi.2012.08.007
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发表时间：
2012-10-01
影响因子：
6.8
通讯作者：
Shimada, Ichio
中科院分区：
文献类型：
--
作者：
Osawa, Masanori;Takeuchi, Koh;Shimada, Ichio
溶液核磁共振波谱可以分析蛋白质在从皮秒到偶数天的大范围时间尺度上的动力学，并以特定位置的方式进行分析，因此其结果与X射线结晶学获得的详细但基本上静态的结构信息是互补的。我们回顾了各种核磁共振技术的最新进展，包括弛豫色散和顺磁弛豫增强(PRE)，这些技术允许观察低密度态，这些态在其他技术中是‘看不见的’。此外，我们还回顾了如何使用核磁共振波谱来阐明与功能相关的蛋白质动力学。
Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been 'invisible' with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics.