DEVELOPMENT OF METHODS OF SINGLE FREQUENCY 2D IR

单频二维红外方法的开发

• 批准号: 8362563
• 负责人: ROBIN Main HOCHSTRASSER
• 金额: $ 13.01万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-06-01 至 2012-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362563
• 关键词: Amides; Amino Acids; Aspartic Acid; Binding; Biomedical Research; Coupling; Development; Environment; Evaluation; Frequencies; Funding; Gases; Glutamic Acid; Goals; Grant; Laboratories; Lysine; Maps; Measurement; Membrane; Methodology; Methods; National Center for Research Resources; Optics; Peptides; Phase; Physiologic pulse; Principal Investigator; Procedures; Process; Property; Protocols documentation; Research; Research Infrastructure; Resources; Secondary Protein Structure; Serine; Shapes; Solid; Solvents; Source; Spectrum Analysis; Structure; Tryptophan; United States National Institutes of Health; Water; amyloid peptide; base; cost; 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. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 该核心是对与肽相关的振动器的原始2D IR实验的延续。主要目标是： - 通过推进和简化回声光谱法的方法，以更快地暴露水和膜环境中肽酰胺基团的附近和其他特性，对2D IR程序的细化，以更将其完整地整合到生物医学研究中。 - 在跨极化方法中的对比度的显着改善，以促进在较大的频率范围内采集跨峰图，该频率范围揭示了肽模式之间的耦合和接近度。 - 通过引入相板，衍射光学元件，相测量和可变形的镜脉冲成型来开发更健壮的2D IR实验。 - 非谐度的2D IR测量及其结构敏感性，角度分布和耦合代表了不同溶剂中蛋白质二级结构的代表，并与气体和分子动力学模拟中发现的蛋白质二级结构进行了比较。 - 开发从C（alpha）-D模式的2D IR获得结构的方法，以提供跨膜肽疏水稳定的方案和理论基础。 - 在13C = 18O或13C后对2D IR光谱的系统评估= 16O替换所有C = O的所有小肽和色氨酸拉链的组，旨在为预测酰胺光谱，零阶模式频率及其离域的预测产生可靠的基础。 -2D IR和线性IR实验，旨在在不同环境中的广泛示例中确定和定居模式的结构和），包括平行和反平行片的同位素，可溶性和膜结合的肽和螺旋，在氧化和螺旋中，氧化和螺旋螺旋体，在氧化和同位素中均为13C = 18O的凝聚者（均为13c = 18O），是无效的，天冬氨酸，丝氨酸，谷氨酸和赖氨酸。