TIME-RESOLVED VIBRATIONAL STUDIES OF PROTEINS

蛋白质的时间分辨振动研究

• 批准号: 2459900
• 负责人: THOMAS S RUSH
• 金额: $ 2.86万
• 依托单位: PRINCETON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-08-01 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/2459900
• 关键词: intermolecular interaction; oxyhemoglobin; posttranslational modifications; protein structure; time resolved data

The proposed research will investigate the dynamics of hemoglobin using time-resolved spectroscopies and computer modeling in order to help determine the molecular mechanism of cooperativity in oxygen binding. This knowledge was intended to be useful for understanding and developing treatments for hemoglobin disorders, for aiding in the design of blood substitutes, and for the understanding of allosteric proteins in general. Important molecular interactions involved in the R to T transition of hemoglobin will be probed using both transient ultraviolet resonance Raman and Fourier transform spectroscopies. The structural information available from the experimental studies will then be used as constraints in various computer simulations aimed at determining intermediate structures and the dynamics of the R to T transition.

拟议的研究将研究血红蛋白的动态 时间分辨的光谱和计算机建模以帮助 确定氧结合中合作的分子机制。 这些知识旨在用于理解和发展 血红蛋白疾病的治疗方法，以帮助血液设计 替代品，以及一般对变构蛋白的理解。 涉及r的重要分子相互作用 血红蛋白将使用两种瞬态紫外线共振进行探测 拉曼和傅立叶变形光谱。结构信息 然后，可以从实验研究中获得作为约束 在旨在确定中间的各种计算机模拟中 R的结构和R到T转变的动力学。