X-RAY STRUCTURES OF DESIGNER PROTEINS

设计蛋白的 X 射线结构

• 批准号: 8363537
• 负责人: STEWART N LOH
• 金额: $ 1.16万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-07-01 至 2012-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363537
• 关键词: Binding; Biosensor; Cells; Chimeric Proteins; Devices; Funding; Grant; Housing; Kinetics; Ligands; Molecular; Molecular Structure; National Center for Research Resources; Optics; Principal Investigator; Protein Binding; Protein Engineering; Proteins; Research; Research Infrastructure; Resolution; Resources; Roentgen Rays; Source; Structure; Thermodynamics; United States National Institutes of Health; Work; X ray diffraction analysis; X-Ray Diffraction; cost; design; dimer; monomer; protein folding

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. The Loh lab specializes in designing proteins to make useful molecular devices or to answer fundamental questions about the thermodynamics and kinetics of protein folding. In some cases it is necessary to determine x-ray structures of the resulting proteins in one or more states to confirm the anticipated structures. The in-house source is not working yet, so we don't have unit cell/space-group/resolution info. We propose to solve the X-ray structures of two classes of engineered protein switches. The first is a two-domain fusion protein which can exist either as a monomer or as a domain-swapped dimer. These molecules are being used to create homotypic protein-protein binding interfaces. The second class is being developed as optical biosensors. These proteins are engineered to undergo a specific conformational change upon binding to ligand. X-ray diffraction will be used to characterize the structures of these molecular switches in their

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。 洛实验室专门设计蛋白质，以制造有用的分子装置或回答有关蛋白质折叠的热力学和动力学的基本问题。在某些情况下，有必要确定所得蛋白质在一种或多种状态下的X射线结构，以确认预期的结构。内部源还没有工作，所以我们没有单位单元/空间组/分辨率信息。 我们建议解决两类工程蛋白质开关的X射线结构。 第一种是双结构域融合蛋白，其可以作为单体或作为结构域交换的二聚体存在。 这些分子被用于创建同型蛋白质-蛋白质结合界面。 第二类正在开发作为光学生物传感器。 这些蛋白质被工程化以在与配体结合时经历特定的构象变化。 X射线衍射将用于表征这些分子开关的结构，