Seidel Karsten, Etzkorn Manuel, Heise Henrike, Becker Stefan, Baldus Marc
Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Chembiochem. 2005 Sep;6(9):1638-47. doi: 10.1002/cbic.200500085.
Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly [13C,15N]-labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the construction of 3D molecular structure and study the influence of solid-phase protein preparation on solid-state NMR spectra. A comparative analysis of 13C', 13Calpha, and 13Cbeta resonance frequencies suggests that 13C chemical-shift variations are most likely to occur in protein regions that exhibit an enhanced degree of molecular mobility. Our results can be refined by additional solid-state NMR techniques and serve as a reference for ongoing efforts to characterize the structure and dynamics of (membrane) proteins, protein complexes, and other biomolecules by high-resolution solid-state NMR.
目前，对于分子间相互作用、分子动力学和样品制备对高分辨率魔角旋转核磁共振数据的影响的理解还很有限。以泛素的均匀[13C,15N]标记样品为例，我们讨论了为构建三维分子结构量身定制的固态核磁共振方法，并研究了固相蛋白质制备对固态核磁共振谱的影响。对13C'、13Calpha和13Cbeta共振频率的比较分析表明，13C化学位移变化最有可能发生在分子流动性增强的蛋白质区域。我们的结果可以通过额外的固态核磁共振技术进行完善，并为目前通过高分辨率固态核磁共振表征（膜）蛋白、蛋白复合物和其他生物分子的结构和动力学的努力提供参考。
