Superconducting NMR Magnet 400 MHz

以下提案的主要目标是用超导磁体替代马丁路德大学哈勒-威滕贝格生物化学和生物技术研究所天然产物生物化学系的400 MHz核磁共振谱仪。该部门专门从事蛋白质和天然产物的生物化学，特别是利用核磁共振波谱解决蛋白质(Re)折叠和稳定、酶设计、多肽合成和介质工程方面的研究问题。400 MHz核磁共振光谱仪是该小组的基本仪器，在正在进行和计划中的研究项目框架中具有核心重要性，这些研究项目旨在阐明高度可调的离子液体与多肽和小蛋白质等复杂生物分子之间的结构-相互作用关系，以及研究酶反应的动力学。为此，对这两种溶液和更具挑战性的高粘度样品进行高分辨率多维核磁共振实验是必要的。有了建立的高分辨率魔角旋转核磁共振工具箱，这样的测量在小组中是可能的。在计划的研究项目中，这项核磁共振技术将进一步应用于监测各种拉长的结构多肽和小蛋白在离子液体中溶解时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，核磁共振波谱还将被用来研究不同离子液体以及溶解在其中的生物分子的动力学，利用它们的弛豫特性。准确表征离子液体与生物催化剂或多肽与蛋白质靶标之间的相互作用将有助于设计特定用途的离子液体。最后，核磁共振波谱将用于研究针对各种抗菌肽的多肽酶的切割偏好，并得出此类酶反应的动力学参数。此外，400 MHz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.