DEVELOPMENT OF METHODS OF SINGLE FREQUENCY 2D IR

单频二维红外方法的开发

• 批准号: 7955429
• 负责人: ROBIN Main HOCHSTRASSER
• 金额: $ 19.17万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-06-01 至 2010-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955429
• 关键词: Amides; Amino Acids; Aspartic Acid; Binding; Biomedical Research; Classification; Computer Retrieval of Information on Scientific Projects Database; Coupling; Development; Environment; Evaluation; Frequencies; Funding; Gases; Glutamic Acid; Goals; Grant; Institution; Laboratories; Lysine; Maps; Measurement; Membrane; Methodology; Methods; Optics; Peptides; Phase; Physiologic pulse; Procedures; Process; Property; Protocols documentation; Research; Research Personnel; Resources; Secondary Protein Structure; Serine; Shapes; Solid; Solvents; Source; Spectrum Analysis; Structure; Tryptophan; United States National Institutes of Health; Water; amyloid peptide; base; method development; molecular dynamics; research study

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This Core is the continuation of the original 2D IR experiments on vibrators associated with peptides. Major goals are: - Refinement of 2D IR procedures in order to more fully integrate them into biomedical research by advancing and simplifying the methodology of echo spectroscopy to more rapidly expose proximities and other properties of peptide amide groups in water and membrane environments. - Significant improvements of the contrast in the crossed polarization method to facilitate the acquisition of cross peak maps over a broad frequency range that exposes coupling and proximities between peptide modes. - Development of more robust 2D IR experiment by introducing phase plates, diffractive optics, phase measurement and deformable mirror pulse shaping into the 2D IR apparatus. - Developments of 2D IR measurements of anharmonicities and their structure sensitivities, angular distributions and couplings representative of protein secondary structures in different solvents and comparisons with those found in gases and molecular dynamics simulations. - Development of approaches for obtaining structure from 2D IR of C(alpha)-D modes to provide the protocols and theoretical underpinning of the hydrophobic stabilization of transmembrane peptides. - Systematic evaluation of 2D IR spectra after 13C=18O or 13C=16O replacement of all C=O groups of some small peptides and tryptophan zippers aimed at generating a solid basis for the prediction of amide spectra, the zero order mode frequencies and their delocalization. - 2D IR and linear IR experiments aimed at structure determination and delocalization of modes in a broad set of examples in different environments including isotopomers of parallel and antiparallel sheets, soluble and membrane bound peptides and helices, aggregates of amyloid peptides and isotopomers of 13C=18O in unusual (non-commercially available as isotopomers) amino acids such as aspartic acid, serine, glutamic acid and lysine.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 该核心是对与肽相关的振动器进行原始 2D IR 实验的延续。主要目标是： - 改进 2D IR 程序，通过推进和简化回波光谱方法，更快速地暴露水和膜环境中肽酰胺基团的邻近性和其他特性，将其更全面地融入生物医学研究中。 - 交叉偏振方法对比度的显着改进，有助于在宽频率范围内获取交叉峰图，从而暴露肽模式之间的耦合和邻近性。 - 通过将相位板、衍射光学、相位测量和可变形镜脉冲整形引入 2D IR 设备，开发更强大的 2D IR 实验。 - 非谐性及其结构灵敏度、代表不同溶剂中蛋白质二级结构的角度分布和耦合的二维红外测量的发展，以及与气体和分子动力学模拟中发现的结果的比较。 - 开发从 C(α)-D 模式的 2D IR 获取结构的方法，为跨膜肽的疏水稳定性提供协议和理论基础。 - 对一些小肽和色氨酸拉链的所有C=O基团进行13C=18O或13C=16O替换后的二维红外光谱的系统评估，旨在为酰胺光谱、零阶模式频率及其离域的预测提供坚实的基础。 - 2D IR 和线性 IR 实验旨在不同环境中的大量示例中的结构确定和模式离域，包括平行和反平行片的同位素异构体、可溶性和膜结合肽和螺旋、淀粉样肽的聚集体和 13C=18O 同位素异构体不常见（非市售同位素）氨基酸，如天冬氨酸、丝氨酸、谷氨酸和赖氨酸。