X-RAY STRUCTURES OF DESIGNER PROTEINS

设计蛋白的 X 射线结构

• 批准号: 8171526
• 负责人: STUART LOH
• 金额: $ 1.13万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-07-01 至 2011-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8171526
• 关键词: Binding; Biosensor; Cells; Chimeric Proteins; Computer Retrieval of Information on Scientific Projects Database; Devices; Funding; Grant; Housing; Institution; Kinetics; Ligands; Molecular; Molecular Structure; Optics; Protein Binding; Protein Engineering; Proteins; Research; Research Personnel; Resolution; Resources; Roentgen Rays; Source; Structure; Thermodynamics; United States National Institutes of Health; Work; X ray diffraction analysis; X-Ray Diffraction; 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. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 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

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 LOH实验室专门设计蛋白质以制造有用的分子设备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，有必要确定一个或多个状态下所得蛋白的X射线结构以确认预期的结构。内部源尚不正常，因此我们没有单元单元/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。 第一个是一种两域融合蛋白，可以作为单体或域交换二聚体存在。 这些分子用于创建同型蛋白质 - 蛋白质结合界面。 第二类是作为光学生物传感器开发的。 这些蛋白质被设计为在与配体结合后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