MACROMOLECULAR DYNAMICS AND ASSEMBLY REACTIONS

大分子动力学和组装反应

• 批准号: 3776280
• 负责人: J HOFRICHTER
• 金额: --
• 依托单位: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3776280
• 关键词: biophysics; carbon monoxide; chemical association; chemical binding; chemical kinetics; chemical models; conformation; cytochrome c; hemoglobin As; hemoprotein structure; laser spectrometry; molecular dynamics; myoglobin; photochemistry; photolysis; protein folding; time resolved data; biophysics; carbon monoxide; chemical association; chemical binding; chemical kinetics; chemical models; conformation; cytochrome c; hemoglobin As; hemoprotein structure; laser spectrometry; molecular dynamics; myoglobin; photochemistry; photolysis; protein folding; time resolved data

Time-resolved absorption spectroscopy is used to study the dynamics of protein structural changes subsequent to excitation with short laser pulses. Molecular models for the protein dynamics are used to fit and interpret the measured data. A. The kinetics of ligand binding and conformational changes for sperm whale myoglobin and human hemoglobin (HbA) have been studied following the photodissociation of carbon monoxide from the hemes. Comprehensive sets of data from partial photolysis experiments using polarized excitation permit cooperative and noncooperative processes to be clearly distinguished. These data also provide accurate measurements of the rotational correlation times of these molecules B. The dynamics of short-lived states on the folding pathway of cytochrome c have been investigated using time-resolved absorption spectroscopy. The binding of carbon monoxide destabilized the folded state of reduced cytochrome c, permitting folding to be initiated by photodissociation of this ligand. We have observed transient binding of other at least two different side chains to the heme subsequent to photodissociation of CO. C. We have disassembled, moved, rebuilt and improved all of the instrumentation used by our laboratory.

时间分辨的吸收光谱用于研究 蛋白质结构变化在激发短激光之后发生 脉冲。 蛋白质动力学的分子模型用于拟合和 解释测量数据。 答：精子的配体结合和构象变化的动力学 鲸鱼肌红蛋白和人类血红蛋白（HBA）已在此之后进行了研究 一氧化碳的光解离。 全面的集合 使用偏光激发许可证的部分光解实验的数据 合作和非合作过程要明确区分。 这些数据还提供了旋转相关性的准确测量 这些分子的时间 B.细胞色素折叠途径上短寿命状态的动力学 使用时间分辨的吸收光谱研究了C。 这 碳一氧化碳的结合不稳定了降低的折叠状态 细胞色素c，允许折叠通过光解离 这个配体。 我们已经观察到其他至少两个的瞬时结合 Co的光解离时的血红素的不同侧链。 C.我们已经拆卸，移动，重建和改进了所有 我们的实验室使用的仪器。