Ban David, Smith Colin A, de Groot Bert L, Griesinger Christian, Lee Donghan
Department of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St., Louisville, KY 40202, USA.
Department for Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, 37077 Germany; Department of Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, 37077 Germany.
Arch Biochem Biophys. 2017 Aug 15;628:81-91. doi: 10.1016/j.abb.2017.05.016. Epub 2017 May 30.
Protein function can be modulated or dictated by the amplitude and timescale of biomolecular motion, therefore it is imperative to study protein dynamics. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique capable of studying timescales of motion that range from those faster than molecular reorientation on the picosecond timescale to those that occur in real-time. Across this entire regime, NMR observables can report on the amplitude of atomic motion, and the kinetics of atomic motion can be ascertained with a wide variety of experimental techniques from real-time to milliseconds and several nanoseconds to picoseconds. Still a four orders of magnitude window between several nanoseconds and tens of microseconds has remained elusive. Here, we highlight new relaxation dispersion NMR techniques that serve to cover this "hidden-time" window up to hundreds of nanoseconds that achieve atomic resolution while studying the molecule under physiological conditions.
蛋白质的功能可由生物分子运动的幅度和时间尺度来调节或决定，因此研究蛋白质动力学势在必行。核磁共振（NMR）光谱是一种强大的技术，能够研究从皮秒时间尺度上比分子重排更快的运动时间尺度到实时发生的运动时间尺度。在整个这一范围内，NMR可观测值能够反映原子运动的幅度，并且可以通过从实时到毫秒以及从几纳秒到皮秒的各种实验技术来确定原子运动的动力学。然而，在几纳秒到几十微秒之间仍有四个数量级的窗口难以捉摸。在此，我们重点介绍新的弛豫色散NMR技术，这些技术有助于覆盖高达数百纳秒的这一“隐藏时间”窗口，在生理条件下研究分子时可实现原子分辨率。
