Superconducting NMR Magnet 400 MHz

以下提案的主要目标是用超导磁体替换哈雷-维滕贝格马丁·路德大学生物化学和生物技术研究所天然产物生物化学系的400兆赫核磁共振光谱仪。该系专门研究蛋白质和天然产物生物化学，特别是在蛋白质（再）折叠和稳定，酶设计，肽合成和介质工程方面的研究问题。400 MHz核磁共振波谱仪是该组必不可少的仪器，在正在进行和计划的研究项目框架中具有核心重要性，旨在阐明高度可调离子液体与复杂生物分子（如肽和小蛋白质）之间的结构相互作用关系，以及研究酶的动力学反应。为此，有必要对溶液和更具挑战性的高粘性样品进行高分辨率多维核磁共振实验。利用已建立的高分辨率魔角旋转核磁共振工具箱，这种测量在小组中是可能的。在计划的研究项目中，该NMR技术将进一步应用于监测各种细长结构肽和小蛋白质在离子液体中溶解后的构象变化和局部结构波动，以及探索离子液体对高度稳定的结构生物分子的影响。除了结构特征外，核磁共振波谱还将通过利用它们的弛豫特性来研究不同离子液体的动力学以及溶解在其中的生物分子。准确表征离子液体与生物催化剂或肽和蛋白质靶点之间的相互作用将有助于设计特定应用的离子液体。最后，核磁共振波谱将应用于研究针对各种抗菌肽的肽酶的裂解偏好，并推导出这些酶促反应的动力学参数。此外，400兆赫核磁共振光谱仪将用于MLU Halle的常规分析测量。

The key objective of the following proposal is a replacement of a superconducting magnet for the 400 MHz NMR spectrometer in the Department of Natural Product Biochemistry at the Institute of Biochemistry and Biotechnology of the Martin Luther University Halle-Wittenberg. The Department specializes in protein and natural products biochemistry and, in particular, addresses research questions in the directions of protein (re)folding and stabilization, enzyme design, peptide synthesis and medium engineering with help of NMR spectroscopy. The 400 MHz NMR spectrometer is an essential instrument in the group and of a central importance in the frames of ongoing and planned research projects aimed at elucidating structure-interaction relationships between highly tuneable ionic liquids and complex biomolecules such as peptides and small proteins, as well as studying kinetic of enzymatic reactions. To that end, the high-resolution multidimensional NMR experiments of both solutions and more challenging highly-viscous samples are necessary. With the established high-resolution magic angle spinning NMR toolbox such measurements were possible in the group. In the planned research projects this NMR technique will be further applied to monitor conformational changes and local structure fluctuations of various elongated structured peptides and small proteins upon dissolving them in ionic liquids, as well as to probe the influence of ionic liquids on highly stable structured biomolecules. In addition to structural features NMR spectroscopy will be used to examine dynamics of different ionic liquids as well as biomolecules dissolved in them by exploiting their relaxation properties. Accurate characterization of interactions between ionic liquids and biocatalysts or peptide and protein targets will facilitate the design of application-specific ionic liquids. Finally, NMR spectroscopy will be applied to address cleavage preferences of peptidases targeting various antimicrobial peptides and kinetic parameters of such enzymatic reactions will be derived. In addition the 400 MHz NMR-Spectrometer will be used for routine analysis measurements in MLU Halle.