Investigating Membrane Proteins with Magnetic Resonance Spectroscopy

用磁共振波谱研究膜蛋白

• 批准号: 1011909
• 负责人: Gary Lorigan
• 金额: $ 42万
• 依托单位: Miami University
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-09-01 至 2014-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1011909&HistoricalAwards=false
• 关键词: Investigating; Membrane; Proteins; Magnetic; Resonance

This research award in the Chemistry of Life Processes (CLP) program, co-funded with the Biomolecular Systems Cluster in the Division of Molecular and Cellular Biosciences, supports work by Professor Gary A. Lorigan at Miami University (Oxford, Ohio) to probe the structure of membrane peptides using Electron Paramagnetic Resonance (EPR) spectroscopy. The objective of the proposed research is to develop state-of-the-art EPR spectroscopic techniques to probe the structural properties of integral membrane peptides. These techniques will be widely applicable to all peptide and protein systems. The pulsed EPR technique of Electron Spin Echo Envelope Modulation (ESEEM) spectroscopy will be used to measure short-range distances ( 8 Angstroms) between a spin label and deuterium nuclei on integral membrane peptides. The ESEEM experiments may become very valuable biophysical tools for measuring distances on chemical and biological systems and will move the field forward by providing an efficient and easy way to distinguish between alpha-helical and beta-sheet structural segments.The potential future benefits of these fundamental studies are to develop new techniques to obtain structural information on membrane proteins. This methodology is useful for all proteins, including those associated with energy transfer, electron transport, photosynthesis, and the consumption and generation of greenhouse gases.

这一生命过程化学(CLP)项目的研究奖是与分子和细胞生物科学部的生物分子系统簇共同资助的，支持迈阿密大学(俄亥俄州牛津)的Gary A.Lrigan教授利用电子顺磁共振(EPR)光谱学探索膜肽的结构。这项研究的目的是开发最先进的EPR波谱技术来探索整膜多肽的结构特性。这些技术将广泛适用于所有的多肽和蛋白质系统。电子自旋回波包络调制(ESEEM)光谱的脉冲EPR技术将被用来测量自旋标记与整体膜多肽上的氢核之间的短距离(8埃)。ESEEM实验可能成为测量化学和生物系统距离的非常有价值的生物物理工具，并将通过提供一种有效和简单的方法来区分α-螺旋和β-折叠结构片段，从而推动该领域的发展。这些基础研究的潜在未来好处是开发新的技术来获得膜蛋白的结构信息。这种方法对所有蛋白质都有用，包括那些与能量转移、电子转移、光合作用以及温室气体的消耗和产生有关的蛋白质。