DEVELOPMENT OF METHODS OF SINGLE FREQUENCY 2D IR

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 这个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： - 改进2D IR程序，以便通过推进和简化回波光谱的方法，更快地暴露肽酰胺基团在水和膜环境中的邻近性和其他性质，将其更充分地整合到生物医学研究中。 - 显著改善交叉极化方法中的对比度，以便于在宽频率范围内采集交叉峰图，从而暴露肽模式之间的耦合和邻近性。 - 通过在二维红外装置中引入相位板、衍射光学、相位测量和变形镜脉冲整形，发展了更鲁棒的二维红外实验。 - 发展二维红外测量的非谐性和它们的结构灵敏度，角分布和耦合代表蛋白质二级结构在不同的溶剂和气体和分子动力学模拟中发现的比较。 - 开发从C（alpha）-D模式的2D IR获得结构的方法，以提供跨膜肽的疏水稳定性的方案和理论基础。 - 系统评价了13 C = 18 O或13 C = 16 O取代某些小肽和色氨酸拉链的所有C=O基团后的二维红外光谱，旨在为预测酰胺光谱、零级模式频率及其离域性提供坚实的基础。 - 2D IR和线性IR实验的目的是在不同环境中的广泛的一组实例中的模式的结构测定和离域，所述实例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不常见的（非市售的同位素异构体）氨基酸如天冬氨酸、丝氨酸、谷氨酸和赖氨酸中的13 C = 18 O的同位素异构体。

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.