Characterization of Solvent-Macromolecule Interactions using Dissolution Dynamic Nuclear Polarization

有了这个新奖项，化学系的化学结构，动力学和机制A计划（CSDM-A）支持教授基督教B。该项目将使用磁共振技术来检查溶液中蛋白质的结构。这些研究将允许确定溶剂（如水）影响蛋白质形状和功能的方式。由于蛋白质在生命过程中起着至关重要的作用，并且通常在水溶液中发挥作用，这些研究将影响分子生物学和生物医学科学的研究。 研究人员还将开发一系列基于网络的模块，针对初中到高中学生，这将突出分子结构在化学和生物学中的重要性。拟议的研究将采用基于核磁共振技术的核超极化来研究位点特异性和时间依赖性溶剂-蛋白质相互作用。将蛋白质与超极化溶剂混合后获得的NMR光谱将揭示转移到蛋白质上的位点的极化。蛋白质上的极化分布将用于推导溶剂结合位点、接触面积和蛋白质结构。

With this new award, the Chemical Structure, Dynamics and Mechanisms A Program (CSDM-A) of the Division of Chemistry supports Professor Christian B. Hilty of Texas A&M University in a project that will use magnetic resonance techniques to examine the structures of proteins in solution. These investigations will allow a determination of the way solvents such as water affect the shape and functions of the proteins they interact with. Since proteins play crucial roles in life processes and often carry out their functions in water solutions, these studies will impact research in molecular biology and the biomedical sciences. The investigator will also develop a series of web-based modules, aimed at middle school to high school students, which will highlight the importance of molecular structure in chemistry and biology. The proposed research will employ nuclear hyperpolarization based NMR techniques to investigate site specific and time dependent solvent-protein interactions. NMR spectra acquired after mixing the protein with hyperpolarized solvent will reveal polarization transferred to sites on the protein. The distribution of polarization on the protein will be used to derive solvent binding sites, contact areas and protein structure.