Solid State NMR Instrument

固体核磁共振仪

• 批准号: 7794568
• 负责人: Robert George Bryant
• 金额: $ 45.1万
• 依托单位: UNIVERSITY OF VIRGINIA
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-02-20 至 2011-08-19
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7794568
• 关键词: Affect; Arts; Bacteria; Biophysics; C2 Domain; Cells; Deuterium; Development; Docking; Event; Infection; Integral Membrane Protein; Lipid Bilayers; Lipids; Magic; Magnetic Resonance Imaging; Mediating; Membrane; Membrane Fusion; Membrane Proteins; Micelles; Molecular; OmpA protein; Physics; Process; Protein Dynamics; Proteins; Protons; Sampling; Site; Solid; Speed; Structure; System; Testing; Water; instrument; instrumentation; opacity protein (Neisseria gonorrhoeae); protein structure; research study; solid state nuclear magnetic resonance

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.

描述（由申请人提供）：该仪器要求是购买一个新的四通道NMR控制台，与现有的11.7 T窄孔超导磁体结合使用，以创建一个新的光谱仪，能够对固体样品进行最先进的NMR实验。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，一个以中等速度旋转。这种组合提供了访问从根本上不同类的实验，允许固体或固体样样品的结构和动力学的研究。静态氘探针的要求，将提供机会，研究当地的动态，特别是氘位点的蛋白质和膜。该仪器的主要应用将是在分子生物物理学的基础蛋白质和完整的膜蛋白质动力学和结构的研究。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中对比度发展的自旋物理学以及受局部水-蛋白质相互作用影响的蛋白质内部能量景观至关重要。它将被应用于检查膜对接的串联C2结构域从synaptotagamin和检查在脂质-蛋白质界面的脂质去混合的问题。这将有助于研究Opa蛋白在双层中的动力学和组装，并提供宿主细胞吞噬细菌的关键识别位点的结构和动力学表征。它将促进膜蛋白相互作用和脂质顺序的膜融合问题的研究，包括SNARE介导的膜融合事件，这对理解感染过程很重要。蛋白OmpA的结构将直接在脂质双层中而不是在胶束支持物中进行研究，以确定最相关的结构，并作为膜蛋白结构测定的最佳方法的关键测试。