An Open-access 800 MHz NMR Spectrometer for Central New England

描述（由申请人提供）：要求为新英格兰中部的研究人员购买一台最先进的开放获取800 MHz核磁共振光谱仪。该仪器将位于康涅狄格州法明顿的康涅狄格大学健康中心，位于Gregory P. Mullen核磁共振结构生物学设施中，该设施目前拥有400、500和600兆赫的光谱仪。该设施由康涅狄格大学支持的全职经理管理。这800人将由来自斯托尔斯和法明顿康涅狄格大学校区、马萨诸塞大学（阿默斯特）、康涅狄格学院、达特茅斯学院、卫斯理大学和耶鲁大学的经验丰富的调查人员组成的核心小组使用，并将向其他人开放。参与调查人员将优先获得访问权限，由多机构调度委员会确定。创始研究小组包括17个实验室，其中12个使用核磁共振作为主要研究工具，并通过其出版记录和外部资助证明了基于核磁共振的蛋白质结构，功能和折叠的杰出研究。800将补充这些研究人员现有的资源，并通过其改进的分辨率和灵敏度，使研究更大、更复杂的系统成为可能。分辨率的提高将来自核共振色散的增加和接近最佳的TROSY效应。对于部分折叠态或具有化学交换的配合物，高场将提高在低场具有中间交换的态之间的分辨率。800将促进用于探测分子动力学的弛豫场依赖研究，并将在国家核磁共振资源进行更高场的实验之前提供初步数据。这800人支持的研究包括参与DNA损伤位点修复和复制的蛋白质、保护DNA免受损伤的蛋白质、蛋白质折叠中间体、分子伴侣、作为肿瘤抑制因子及其突变体的蛋白质、动力蛋白分子运动蛋白、在细胞分裂中起作用的蛋白质、2肾上腺素能受体、细胞信号蛋白、参与抗生素耐药性的酶、造血细胞因子及其受体、以及多域神经突生长起始因子。

DESCRIPTION (provided by applicant): Support for the acquisition of a state-of-the-art open-access 800 MHz NMR spectrometer for researchers in central New England is requested. The instrument will be located at the University of Connecticut Health Center in Farmington, CT, in the Gregory P. Mullen NMR Structural Biology Facility, which currently houses spectrometers operating at 400, 500, and 600 MHz. The Facility is operated by a full-time manager supported by the University of Connecticut. The 800 will be utilized by a core group of experienced investigators from the Storrs and Farmington UConn campuses, the University of Massachusetts (Amherst), Connecticut College, Dartmouth College, and Wesleyan and Yale Universities, and will be available to others. Participating investigators will obtain access on a priority basis, determined by a multi-institution scheduling committee. The founding group of investigators comprises 17 laboratories, 12 of which use NMR as a primary research tool, and has demonstrated outstanding NMR-based research into protein structure, function, and folding through its record of publication and external funding. The 800 will complement the existing resources available to these researchers and will enable the investigation of larger, more complex systems through its improved resolution and sensitivity. Gains in resolution will result both from the increased dispersion of nuclear resonances and from near-optimal TROSY effects. For partially folded states or complexes exhibiting chemical exchange, the higher field will improve resolution between states that show intermediate exchange at lower field. The 800 will facilitate field-dependent studies of relaxation used to probe molecular dynamics, and will provide preliminary data prior to experiments at higher field conducted at the national NMR resources. Studies to be supported by the 800 include proteins that participate in repair and replication at the sites of DNA damage, proteins that protect from DNA damage, protein folding intermediates, molecular chaperones, proteins that function as tumor suppressors and their mutants, dynein molecular motor proteins, proteins that function in cell division, the 2 adrenergic receptor, cell signaling proteins, enzymes involved in antibiotic resistance, hemopoeitic cytokines and their receptors, and multi- domain neurite outgrowth initiation factors.