600 MHz NMR Spectrometer for Shared Use

描述（由申请人提供）：要求在约翰霍普金斯大学霍姆伍德校区使用一台高场NMR光谱仪，其1H共振频率为600 MHz，设备齐全，可用于生物分子应用，以满足广泛的生物物理和生物化学研究人员的需求。所要求的仪器将设在一个新完成的NMR中心，根据该大学的长期目标，为生物分子结构和动力学的基础研究提供最先进的能力。这种仪器将显着受益于生物，生物物理和化学，其中六个是NIH资助的部门的七个院系的研究计划。介绍了一系列具有生物学、生物物理学和化学意义的研究项目：（1）线粒体分裂相关蛋白质的结构和动力学研究。(2)核磁共振研究大分子结构和动力学及其与生物功能的关系。(3)氨基酸多态性和突变导致HIV-1蛋白酶耐药的长期效应(4)膜蛋白的结构和能量原理。(5)蛋白质结构与能量的相关性。(6)AraC的DNA结合结构域的结构测定及其同源DNA存在和不存在下的动力学。(7)DNA结合蛋白在有无DNA存在下主链和侧链动力学的热力学分析。

DESCRIPTION (provided by applicant): A high-field NMR spectrometer, operating at a 1H resonance frequency of 600 MHz and fully equipped for biomolecular applications, is requested to meet the needs of a broad group of biophysical and biochemical investigators at the Homewood campus at Johns Hopkins University. The requested instrumentation will be sited in a newly completed NMR Center, constructed in accordance with the University's long term goal of providing state-of-the-art capabilities for fundamental investigations of biomolecular structure and dynamics. This instrumentation will significantly benefit the research programs of seven faculties from the Departments of Biology, Biophysics, and Chemistry, of which six are NIH-funded. A range of projects of biological, biophysical, and chemical significance are described: (1) Structure and dynamics studies of proteins involved in mitochondrial division. (2) NMR studies of macromolecular structure and dynamics and its relationship to biological function. (3) Long range effects of amino acid polymorphisms and mutations causing drug-resistant in the HIV-1 protease. (4) Structural and energetic principles of membrane proteins. (5) Correlation between structure and energy in proteins. (6) Structure determination of the DNA-binding domain of AraC and dynamics in the presence and absence of its cognate DNA. (7) Thermodynamic analysis of backbone and side chain dynamics of DNA binding proteins in the presence and absence of DNA.