Solid State NMR Instrument

描述（由申请人提供）：该仪器要求是购买一个新的四通道核磁共振控制台，与现有的11.7 T窄孔超导磁体一起使用，以创建一个新的光谱仪，能够对固体样品进行最先进的核磁共振实验。需要三个新的探针：两个魔角旋转探针，一个以最高速度旋转，一个以中速旋转。这种结合提供了从根本上不同类别的实验，允许研究固体或类固体样品的结构和动力学。需要一种静态氘探针，这将为研究蛋白质和膜中特定氘化位点的局部动力学提供机会。该仪器的主要应用将是分子生物物理学，用于研究基本蛋白和整体膜蛋白的动力学和结构。该仪器将促进蛋白质系统中质子自旋动力学的研究，这对于理解MRI中造影剂发展的自旋物理以及受局部水-蛋白质相互作用影响的蛋白质内部能量景观至关重要。它将用于检查突触他他明串联C2结构域的膜对接，并检查脂质-蛋白界面的脂质分离问题。这将有助于研究双分子层中蛋白的动力学和组装，并为宿主细胞吞噬细菌的关键识别位点提供结构和动力学表征。这将有助于研究膜-蛋白相互作用和膜融合问题中的脂质顺序，包括对理解感染过程很重要的snare介导的膜融合事件。OmpA蛋白的结构将直接在脂质双分子层中进行研究，而不是在胶束支架中进行研究，以确定最相关的结构，并作为膜蛋白结构确定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.