INTRINSIC FLUORESCENCE DECAY MECHANISMS OF PROTEINS

蛋白质的固有荧光衰减机制

• 批准号: 3296907
• 负责人: J B ALEXANDER ROSS
• 金额: $ 12.51万
• 依托单位: MOUNT SINAI SCHOOL OF MEDICINE OF CUNY
• 依托单位国家: 美国
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-07-01 至 1992-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3296907
• 关键词: X ray crystallography; chemical structure function; conformation; electronic spectra; fluorescence; insulin; mathematical model; nuclear magnetic resonance spectroscopy; oxytocin; peptides; phenylalanine; protein engineering; protein structure; solutions; tryptophan; tyrosine analog

Intrinsic Fluorescence Decay Mechanisms of Proteins is a multi- investigator, multidisciplinary project combining time-resolved fluorescence with NMR and molecular modeling. Our objective is to determine how time-resolved fluorescence of the three aromatic amino acids tryptophan, tyrosine, and phenylalanine can be used to obtain information about structure and conformational dynamics of proteins. This requires understanding how and to what extent ground-state and excited-state processes affect the fluorescence intensity decay kinetics. NMR is being used to help define important ground-state processes. Molecular modeling, based on X- ray crystal structures, is being used to compute properties of an aromatic amino acid's local environment for comparison with the conclusions obtained from fluorescence and NMR. In this initial grant period we are investigating well-defined, simple peptide and polypeptide analogues having a single aromatic amino acid by systematically substituting in each aromatic amino acid at the same position in the peptide chain. These studies on peptides and polypeptides are the basis for extending the investigation into several structurally related single-tyrosine proteins. The results of this interdisciplinary approach, emphasizing tyrosine fluorescence, will be used, through a continuation application, to extend this investigation to tryptophan fluorescence of proteins. This work will further our understanding of the time-resolved fluorescence of the aromatic residues, add significantly to our knowledge of the solution structure and conformational dynamics of proteins, and make time-resolved fluorescence techniques a more powerful tool for analyzing protein structure.

蛋白质的固有荧光衰变机制是一个多因素 研究者，结合时间分辨的多学科项目 核磁共振和分子建模的荧光。 我们的目标是 确定三种芳香族化合物的时间分辨荧光如何 氨基酸色氨酸、酪氨酸和苯丙氨酸可用于 获得有关结构和构象动力学的信息 蛋白质。 这需要了解如何以及在何种程度上 基态和激发态过程影响荧光 强度衰减动力学。 NMR 被用来帮助定义 重要的基态过程。 分子建模，基于X- 射线晶体结构，被用来计算 芳香族氨基酸的局部环境与 从荧光和NMR得出的结论。 在这个最初的 资助期我们正在研究明确的、简单的肽和 具有单一芳香族氨基酸的多肽类似物 在同一位置系统地取代每个芳香族氨基酸 肽链中的位置。 这些关于肽和 多肽是扩展研究的基础 几种结构相关的单酪氨酸蛋白。 结果 这种跨学科方法，强调酪氨酸 荧光，将通过持续应用用于 将这项研究扩展到蛋白质的色氨酸荧光。 这项工作将进一步加深我们对时间分辨的理解 芳香族残基的荧光，显着增加我们的 溶液结构和构象动力学的知识 蛋白质，并使时间分辨荧光技术更加 分析蛋白质结构的强大工具。