Cryoprobe Accessory for a 600 MHz NMR Spectrometer

描述（由申请人提供）：位于阿拉巴马大学伯明翰分校核磁共振共享设施的600 MHz核磁共振光谱仪（Bruker Avance-600）目前为校园内的教职员工提供了最高的操作场。它被各种各样的研究人员使用，从需要高灵敏度检测的痕量化合物的表征到通过3D/4D-NMR光谱测定蛋白质的三维结构。为了显着提高该仪器在适应这些生物分子系统研究项目中的效率，要求为600 MHz核磁共振系统购买三共振逆冷冻探针附件。与传统的室温探头相比，该探头的灵敏度提高了300%至400%（取决于样品），并将显著提高600 MHz核磁共振光谱仪的能力，以满足UAB校园的需求。随着灵敏度的显著提高，该仪器可以：(i)减少对同位素标记蛋白质进行3D/4D-NMR测量的数据采集时间，从几周或几个月减少到几天，（ii）增加NMR样品的吞吐量，（iii）允许研究仅在低浓度下可用或仅少量可溶的生物分子，（iv）允许结构研究具有有限生命时间的蛋白质和化合物。(v)允许在mM浓度下倾向于二聚体，但在低浓度下主要是单体的蛋白质的结构表征。此次600 MHz CryoProbe升级将对一个主要用户组的项目产生重大影响，该用户组由8名教师组成，他们的研究项目涉及人类载脂蛋白a - 1、干扰素-tau、心肌调节蛋白、钙调素与HIV gp41的相互作用、噬菌体P22支架蛋白、药物/DNA复合物、从炭素芽孢杆菌中分离的表面寡糖。低浓度代谢中间体的1H和isc表征。

DESCRIPTION (provided by applicant): The 600 MHz NMR Spectrometer (Bruker Avance-600) at the NMR Shared Facility of the University of Alabama at Birmingham currently provides the highest operating field available for the faculty members on the campus. It is being utilized by a diverse group of investigators working on projects ranging from the characterization of trace amounts of compounds requiring high sensitivity detection to the three dimensional structure determinations of proteins by 3D/4D-NMR spectroscopy. To significantly enhance the efficiency of this instrument in accommodating these research projects on biomolecular systems, a request is made for the purchase of a triple resonance inverse CryoProbe accessory for the 600 MHz NMR system. This probe provides a sensitivity enhancement of 300% to 400% (depending upon the sample) over the conventional room temperature probe, and will dramatically and significantly enhance the capabilities of the 600 MHz NMR spectrometer in meeting the needs of the UAB campus. With the significant improvement in sensitivity, the instrument can :(i) reduce data acquisition times for 3D/4D-NMR measurements on isotopically labeled proteins from several weeks or months to just a few days, (ii) increase the through-put of NMR samples, (iii) permit the study of biomolecules that are available only in low concentrations or only sparingly soluble, (iv) permit the structural study of proteins and compounds that have a limited life time, and (v) permit the structural characterization of proteins that tend to dimerize at mM concentrations but are predominantly monomeric at low concentrations. This 600 MHz CryoProbe upgrade will have a significant impact upon the programs of a major user group consisting of eight faculty members with research projects dealing with multidimensional NMR structural investigations on human apolipoprotein A-l, interferon-tau, cardiac muscle regulatory proteins, interaction of calmodulin with HIV gp41, bacteriophage P22 scaffolding protein, drug/DNA complexes, surface oligosaccahrides isolated from the Bacillus anthracis Exosporium, and the 1H and ISC-characterization of metabolic intermediates in low concentration.