MACROMOLECULAR INTERACTIONS SHARED RESOURCE

大分子相互作用共享资源

基本信息

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
项目类别：
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

项目摘要

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研究人员提供了最新进展用于表征蛋白质-蛋白质、蛋白质-脂质、蛋白质-核酸和蛋白质-小分子的艺术能力分子相互作用。该设施为大分子的完整表征提供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的互动。表面等离子共振 (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、结合位点和表位作图。分析超速离心 (AUG) 的优势包括表征分子量分布和球形程度的能力同时测定大分子混合物，并测定单个溶质的部分浓度，帮助研究构象变化和样品组成、溶液分子质量，组装复合物的化学计量，并为自缔合提供严格的热力学系统。静态和动态光散射（LS）是研究尺寸和尺寸的有用工具细胞、病毒、胶束和大分子（例如蛋白质、大分子组装体）的分布多糖、核酸。 LS 对于大分子组装和动力学研究也很有用实时拆解。通过在单个共享资源中提供所有这些生物物理工具设施，我们能够为我们的癌症中心研究人员提供极高水平的严谨和大分子复合物和药物靶点研究的复杂性已成为如此现代癌症研究的重要组成部分。