UV RESONANCE RAMAN STUDIES OF PROTEIN STRUCTURE

蛋白质结构的紫外共振拉曼研究

• 批准号: 6018559
• 负责人: SANFORD A. ASHER
• 金额: $ 26.4万
• 依托单位: UNIVERSITY OF PITTSBURGH AT PITTSBURGH
• 依托单位国家: 美国
• 财政年份: 1982
• 资助国家: 美国
• 起止时间: 1982-06-01 至 2002-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6018559
• 关键词: Raman spectrometry; bioengineering /biomedical engineering; biomedical equipment development; chemical models; cis trans isomerization; laser spectrometry; myoglobin; optics; peptides; photochemistry; protein folding; protein structure function; structural biology

The work proposed will develop UV resonance Raman spectroscopy (UVRS) as an incisive technique to examine protein structure and function. We will apply this technique for fundamental studies of amide, peptide and protein excited states and will search for delocalized electronic transitions similar to our recently discovered peptide charge transfer transitions. We will use a photochemical isomerization switching mechanism to determine the amino acid side chain dependence of the ground state trans yields cis peptide activation barriers. We will develop and utilize static and kinetic nsec-msec UVRS methods to examine the unfolding intermediates of proteins such as myoglobin (Mb) and apoM. We will, characterize the dynamical connectivities between adjacent peptide bonds by selectively initiating trans yields cis isomerization in a thioamide substituted peptide, and then measure the conformational changes at adjacent peptide bonds. We will improve UV Raman instrumentation, to increase its sensitivity.

提出的工作将发展UV共振拉曼光谱法（UVRS） 作为检查蛋白质结构和功能的敏锐技术。 我们 将把这种技术应用于酰胺，肽和 蛋白质激发态，将搜索DELEACALIZED电子 类似于我们最近发现的肽电荷转移的过渡 过渡。 我们将使用光化学异构化切换 确定氨基酸侧链依赖性的机制 基态反式产生顺式肽激活屏障。 我们将 开发和利用静态和动力学NSEC-MSEC UVRS方法来检查 蛋白质（例如肌红蛋白（MB）和APOM）的展开中间体的展开中间体。 我们将表征相邻的动态连接 肽键通过选择性启动trans产生CIS异构化。 在硫酰胺取代的肽中，然后测量构象 相邻肽键的变化。 我们将改善紫外拉曼 仪器，以提高其灵敏度。