Solid State NMR Instrument

描述(申请人提供)：本仪器申请购买一台新的四通道核磁共振控制台，与现有的11.7T窄孔超导磁体配合使用，以创建一台能够在固体样品上进行最先进的核磁共振实验的新光谱仪。需要三个新的探头：两个魔角旋转探头，一个以最高速度旋转，一个以中速旋转。这种组合提供了进入根本不同类别的实验的途径，这些实验允许研究固体或类固体样品的结构和动力学。需要一个静态的氚探头，它将提供机会来研究蛋白质和膜中特定的氚位置的局部动力学。该仪器的主要应用将是研究基础蛋白质和整体膜蛋白质的动力学和结构的分子生物物理学。该仪器将有助于研究蛋白质系统中的质子-自旋动力学，这对于理解磁共振成像中对比度发展的自旋物理以及蛋白质中受局部水-蛋白质相互作用影响的内部能量格局至关重要。它将被用来研究从突触素串联的C2结构域的膜对接，以及研究脂-蛋白质界面的脂解混问题。它将有助于研究OpA蛋白在双层中的动态和组装，并提供宿主细胞吞噬细菌的关键识别位点的结构和动态特征。这将有助于研究膜-蛋白质相互作用和膜融合问题中的脂质顺序，包括SNARE介导的膜融合事件，这对理解感染过程是重要的。OmpA蛋白的结构将直接在脂质双层中而不是在胶束载体中进行研究，以确定最相关的结构，并作为确定膜蛋白结构的最佳方法的关键测试。

DESCRIPTION (provided by applicant): This instrumentation request is to purchase a new four-channel NMR console to be used in conjunction with an existing 11.7 T narrow bore super conducting magnet to create a new spectrometer capable of state-of-the-art NMR experiments on solid samples. Three new probes are requested: two magic angle spinning probes, one to spin at the highest speeds and one at intermediate speeds. This combination provides access to fundamentally different classes of experiments that permit study of both structure and dynamics for solid or solid-like samples. A static deuterium probe is requested that will provide opportunities to study local dynamics of specifically deuterated sites in proteins and membranes. The primary applications of this instrument will be in molecular biophysics for the study of fundamental protein and integral membrane protein dynamics and structure. This instrument will facilitate the study of proton-spin dynamics in protein systems that are critical to understanding the spin-physics of contrast development in MRI as well as the internal energy landscape in proteins as affected by local water- protein interactions. It will be applied to examine membrane docking of tandem C2 domains from synaptotagamin and to examine the problem of lipid de-mixing at the lipid-protein interface. It will facilitate studies of the dynamics and assembly of the Opa proteins in bilayers and provide structural and dynamical characterization of the key recognition sites for engulfment of bacteria by the host cells. It will facilitate studies of membrane-protein interactions and lipid order in membrane fusion problems including SNARE-mediated membrane fusion events that are important in understanding the infection process. The structure of the protein OmpA will be studied directly in lipid bilayers rather than in micelle supports to determine the most relevant structure and serve as a key test of optimal approaches to structure determination for membrane proteins.