MACROMOLECULAR INTERACTIONS SHARED RESOURCE

大分子相互作用共享资源

• 批准号: 8637194
• 负责人: EILEEN M. LAFER
• 金额: $ 1.96万
• 依托单位: UNIVERSITY OF TEXAS HLTH SCIENCE CENTER
• 依托单位国家: 美国
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-08-01 至 2014-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8637194
• 关键词: Affinity; Amines; Antibodies; Basic Science; Binding; Binding Sites; Biological; Biotin; Cancer Center; Cell Extracts; Cells; Chemistry; Complex; Consumption; Couples; Coupling; Data; Detection; Diffusion; Dissociation; Drug Targeting; Epitope Mapping; Equilibrium; Event; Gold; Hydrophobic Interactions; Individual; Kinetics; Label; Lipids; Macromolecular Complexes; Malignant Neoplasms; Measures; Micelles; Molecular; Molecular Weight; NCI Center for Cancer Research; Names; Nucleic Acids; Play; Polysaccharides; Preclinical Drug Evaluation; Proteins; Radial; Research Personnel; Resource Sharing; Resources; Role; Sampling; Services; Solutions; Speed; Surface; Surface Plasmon Resonance; System; Thermodynamics; Time; Virus; Weight; Weights and Measures; analytical ultracentrifugation; anticancer research; assay development; base; cancer therapy; carboxyl group; drug development; drug discovery; instrumentation; interest; light scattering; macromolecular assembly; macromolecule; member; molecular mass; particle; polypeptide; research study; sedimentation equilibrium; sensor; small molecule; solute; stoichiometry; tool

The Macromolecular Interactions Shared Resource provides Cancer Center researchers with state-of-the art capabilities for the characterization of protein-protein, protein-lipid, protein-nucleic acid and protein-small molecule interactions. The facility provides resources for the complete characterization of macromolecular interactions in solution. This includes a description of the kinetics, thermodynamics and assembly state of the interaction. The strengths of surface plasmon resonance (SPR) include the determination of binding kinetics and equilibria, the determination of active protein concentrations, assay development and drug screening, and binding site and epitope mapping. The strengths of analytical ultracentrifugation (AUG) include the ability to characterize distributions of molecular weight and degree of globularity for macromolecular mixtures simultaneously, and to determine the partial concentration of individual solutes, aiding in the study of conformational changes and sample composition, solution molecular mass, stoichiometry of assembled complexes, and providing rigorous thermodynamics for self-associating systems. Static and dynamic light scattering (LS) are useful tools in the study of the size and size distribution of cells, viruses, micelles, and macromolecules such as proteins, macromolecular assemblies, polysaccharides, and nucleic acids. LS is also useful for the kinetic study of macromolecular assembly and disassembly in real time. By having all of these biophysical tools available in a single shared resource facility, we are able to offer our Cancer Center researchers an extraordinarily high level of rigor and sophistication for the study of the macromolecular complexes and drug targets that have become such an important part of modern cancer research.

大分子相互作用共享资源为癌症中心的研究人员提供了国家的 具有表征蛋白质-蛋白质、蛋白质-脂质、蛋白质-核酸和蛋白质-小分子的能力 分子相互作用该设施为大分子的完整表征提供了资源 溶液中的相互作用这包括动力学，热力学和组装状态的描述， 互动。表面等离子体共振（SPR）的优势包括结合的测定 动力学和平衡，活性蛋白浓度的测定，测定开发和药物 筛选和结合位点和表位作图。分析超离心（AUG）的优势 包括表征分子量分布和球形度的能力， 大分子混合物的同时，并确定个别溶质的部分浓度， 有助于研究构象变化和样品组成，溶液分子量， 组装复合物的化学计量，并提供严格的热力学自缔合 系统.静态和动态光散射（LS）是研究尺寸和大小的有用工具 细胞、病毒、胶束和大分子如蛋白质，大分子组装体， 多糖和核酸。LS还可用于大分子组装的动力学研究， 真实的拆卸。通过将所有这些生物物理工具集中在一个共享资源中， 我们能够为癌症中心的研究人员提供非常高水平的严谨性， 复杂的大分子复合物和药物靶点的研究，已成为这样一个 现代癌症研究的重要组成部分。