STRUCTURE AND FUNCTION OF THE OUTER HAIR CELL MOTOR PROTEIN, PRESTIN

外毛细胞运动蛋白 PRESTIN 的结构和功能

• 批准号: 8361580
• 负责人: ALBERT JAMES HUDSPETH
• 金额: $ 1.3万
• 依托单位: ROCKEFELLER UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8361580
• 关键词: Azides; Binding; Binding Sites; Carboxylic Acids; Collaborations; Data Analyses; Funding; Grant; Ligands; Mass Spectrum Analysis; Measurement; Mechanics; Motor; National Center for Research Resources; Outer Hair Cells; Photoaffinity Labels; Principal Investigator; Proteins; Research; Research Infrastructure; Resources; Source; Structure; Techniques; United States National Institutes of Health; Work; cost; macromolecule; rat Pres protein

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. Fisher is utilizing photoaffinity labeling, mechanical measurements, and, in collaboration with our lab, mass spectrometry to elucidate the structure and function of the outer hair cell motor protein, prestin. Because the azide-modified ligand that he is working with appears to bind to prestin with remarkable efficiency, it is likely that he will be able to identify covalently modified residues by using mass spectrometric and data analysis techniques that my lab has developed. This will permit him to investigate prestin's putative binding site for small carboxylic acids.

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。 Fisher正在利用光亲和标记、机械测量以及与我们实验室合作的质谱分析来阐明外毛细胞运动蛋白普雷斯廷的结构和功能。 由于他所研究的叠氮化物修饰配体似乎能以显著的效率与普雷斯廷结合，因此他很可能能够通过使用我的实验室开发的质谱和数据分析技术来识别共价修饰的残基。这将使他能够研究普雷斯廷与小分子羧酸的假定结合位点。