Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-St. 10, 13125 Berlin-Buch, Germany.
J Am Chem Soc. 2010 Jul 7;132(26):8891-3. doi: 10.1021/ja102612m.
Structural investigations are a prerequisite to understand protein function. Intermediate time scale motional processes (ns-micros) are deleterious for NMR of biological solids and obscure the detection of amide moieties in traditional CP based solid-state NMR approaches as well as in regular scalar coupling based experiments. We show that this obstacle can be overcome by using TROSY type techniques in triple resonance experiments, which enable the assignment of resonances in loop regions of a microcrystalline protein. The presented approach provides an exemplified solution for the analysis of secondary structure elements undergoing slow dynamics that might be particularly crucial for understanding protein function.
结构研究是理解蛋白质功能的前提。中间时间尺度的运动过程（ns-微秒）对生物固体的 NMR 是有害的，并掩盖了在传统基于 CP 的固态 NMR 方法以及在常规标量耦合实验中酰胺部分的检测。我们表明，通过在三共振实验中使用 TROSY 类型的技术可以克服这一障碍，这使得在微晶蛋白质的环区中分配共振成为可能。所提出的方法为分析经历缓慢动力学的二级结构元件提供了一个例证解决方案，这对于理解蛋白质功能可能尤为关键。
