Raman Spectroscopy and Pressure Studies of Protein Dynamics

蛋白质动力学的拉曼光谱和压力研究

• 批准号: 9305711
• 负责人: Alfons Schulte
• 金额: $ 19.92万
• 依托单位: The University of Central Florida Board of Trustees
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-08-01 至 1997-07-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9305711&HistoricalAwards=false
• 关键词: Raman; Spectroscopy; Pressure; Studies; Protein

9305711 Schulte Variations in pressure and temperature are combined with time- resolved Raman spectroscopy to study reaction parameters and motions relevant for protein function. The principal focus is on two prototype processes: ligand binding to myoglobin and light energy transduction in the proton-pump bacteriorhodopsin. The protein is brought to a particular state of the Gibbs free energy surface by changing pressure and temperature. A sudden external perturbation, for instance a pressure jump or a laser flash, initiates a reaction or a relaxation. Kinetic studies of vibrational modes that change in position and intensity explore the highly degenerate energy surface and relaxation phenomena. In addition to monitoring Raman bands in the visible we use excitation in the near-infrared to obtain Raman spectra in the absence of undesired photochemistry and resonance enhancement. These investigations provide new information on the arrangement of the conformational energy surface in myoglobin and bacteriorhodopsin, pressure effects on protein dynamics and on the molecular structure of bacteriorhodopsin activation. %%% The dynamics structures which proteins maintain to perform biological functions are distinguished by changes in energy and volume from the unfolded polypeptide chain. Site-selective spectroscopic studies at variable temperature and pressure provide insight into the relative energy scales of molecular interactions in the stabilization of the biologically active molecule. Vibrational marker bands are used to monitor structural changes and motions in myoglobin and bacteriorhodopsin and correlate them with protein function. Since proteins share similarities in the thermodynamic, structural and dynamic properties with many disordered systems such as glasses, new insights from this research will have an impact on models for disorder and complexity in other fields of science. ***

9305711舒尔特压力和温度的变化与时间分辨拉曼光谱相结合，研究与蛋白质功能相关的反应参数和运动。主要集中在两个原型过程：配体与肌红蛋白的结合和质子泵细菌视紫红质中的光能转导。通过改变压力和温度，蛋白质被带到吉布斯自由能表面的特定状态。突然的外部扰动，例如压力跳跃或激光闪光，会引发反应或松弛。对位置和强度变化的振动模的动力学研究探索了高度简并的能面和弛豫现象。除了监测可见光中的拉曼光谱外，我们还利用近红外的激发来获得拉曼光谱，而不需要进行不必要的光化学和共振增强。这些研究为肌红蛋白和细菌视紫红质的构象能面排列、压力对蛋白质动力学的影响以及细菌视紫红质激活的分子结构提供了新的信息。蛋白质执行生物功能所维持的动力学结构是由未折叠的多肽链的能量和体积的变化来区分的。在可变温度和压力下的位置选择性光谱研究提供了对分子相互作用在生物活性分子稳定中的相对能量尺度的洞察。振动标记带用于监测肌红蛋白和细菌视紫红质的结构变化和运动，并将它们与蛋白质功能相关联。由于蛋白质在热力学、结构和动力学性质上与许多无序系统(如玻璃)相似，因此这项研究的新见解将对其他科学领域的无序和复杂性模型产生影响。***