HEME PROTEIN STRUCTURE AND DYNAMICS

血红素蛋白结构和动力学

• 批准号: 2828893
• 负责人: THOMAS G. SPIRO
• 金额: $ 8.32万
• 依托单位: PRINCETON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1979
• 资助国家: 美国
• 起止时间: 1979-04-01 至 1998-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2828893
• 关键词: Raman spectrometry; adduct; amine oxidoreductase; chemical models; computer simulation; cytochrome c; guanylate cyclase; heme; hemoprotein structure; infrared spectrometry; miscellaneous oxidoreductase; molecular dynamics; myoglobin; nitric oxide; nitrites; porphyrins; protein folding; protein structure function; Raman spectrometry; adduct; amine oxidoreductase; chemical models; computer simulation; cytochrome c; guanylate cyclase; heme; hemoprotein structure; infrared spectrometry; miscellaneous oxidoreductase; molecular dynamics; myoglobin; nitric oxide; nitrites; porphyrins; protein folding; protein structure function

Structural and functional studies will be carried out in order to provide a molecular-level understanding of the role of heme proteins in fundamental physiological processes, including respiration metabolism, and the regulation of cellular responses. Resonance Raman spectroscopy will be applied as a structural monitor of the heme group, and of its interaction with proteins and with exogenous ligands, including especially the newly discovered signaling molecule NO. Computer modeling with a high quality force field will be employed in order to extract maximum information from the spectra.

将进行结构和功能研究以提供 分子级的理解血红素蛋白在 基本的生理过程，包括呼吸代谢和 细胞反应的调节。共振拉曼光谱将是 用作血红素组及其相互作用的结构监视器 蛋白质和外源配体，尤其是新近的配体 发现的信号分子no。高质量的计算机建模 将采用力场来从中提取最大信息 光谱。