Development of a Very High Field Solid-state NMR Spectrometer

9977682 opella这个项目是开发一个非常高场核磁共振光谱仪，将专门用于测定生物超分子结构中的蛋白质结构，包括膜和病毒颗粒。该光谱仪将在最高可用的共振频率下工作，并将执行全范围的高分辨率固态核磁共振实验，以对均匀标记的蛋白质样品的单个共振的光谱参数进行分辨率，分配和测量。特别是膜蛋白的结构，在蛋白质数据库的已知结构中，由于传统的x射线晶体学和溶液核磁共振方法存在技术困难，膜蛋白的结构在蛋白质数据库中的代表性大大不足。这些蛋白质在溶液中结晶和重新定向的速度不会太慢。核磁共振测定蛋白质结构、表征动力学、描述化学性质和相互作用的能力取决于电子元件的能力，尤其是外加磁场的强度。使用最强的可用磁铁的优势是不成比例的大，因为在灵敏度，分辨率和控制相关的协同改进。该小组计划购买可用的最高磁场磁铁，并开发相关仪器，特别是探针，用于通过固态核磁共振光谱测定蛋白质结构的研究光谱仪。初步结果表明，在700 ~ 1100mhz频率范围内构建和调谐高功率双共振和三共振探头是可行的。这将对未来几代光谱学家产生重大影响，因为大部分开发和实验工作将由宾夕法尼亚大学蛋白质固态核磁共振资源的研究生和博士后研究助理进行。

9977682OpellaThis project is to develop a very high field NMR spectrometer that will be dedicated to the determination of structure of proteins in biological supra-molecular structures, including membranes and virus particles. The spectrometer will operate at the highest available resonance frequencies and will perform the full range of high-resolution solid-state NMR experiments needed for the resolution, assignment and measurement of spectroscopic parameters of individual resonances from uniformly labeled protein samples. The structures of membrane proteins, in particular, are vastly under-represented among known structures in the Protein Data Bank because of the technical difficulties they present for conventional x-ray crystallographic and solution NMR methods. These proteins do not crystallize and reorient too slowly in solution. The ability of NMR to determine protein structure, characterize dynamics and describe chemical properties and interactions depends on the capabilities of the electronic components and, especially, the strength of the applied magnetic field. The advantages of using the strongest available magnet are disproportionately large because of the associated synergistic improvements in sensitivity, resolution and control.The group plans to purchase the highest field magnet available, and to develop the associated instrumentation, especially the probes, for a research spectrometer optimized for protein structure determination by solid state NMR spectroscopy. Preliminary results demonstrate the feasibility of constructing and tuning high power double-and triple-resonance probes for frequencies in the range of 700 to 1100 MHz. There will be substantial impact on future generations of spectroscopists because much of the development and experimental work will be performed by graduate students and postdoctoral research associates at the Resource for Solid-State NMR of Proteins at the University of Pennsylvania.