NMR OF PROTEIN-CARBOHYDRATE INTERACTIONS USING FIELD-INDUCED ALIGNMENT

使用场诱导排列的蛋白质-碳水化合物相互作用的核磁共振

• 批准号: 7358184
• 负责人: JAMES H. PRESTEGARD
• 金额: $ 0.14万
• 依托单位: UNIVERSITY OF GEORGIA
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-02-01 至 2007-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7358184
• 关键词: NMR; PROTEIN; CARBOHYDRATE; INTERACTIONS; USING

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. Anisotropic NMR parameters such as residual dipolar couplings can provide valuable orientational constraints on the bound-state geometry of carbohydrates that interact with proteins. However, methods must be developed that allow bound-state information to dominate averages observed in rapidly exchanging systems. Field induced orientation of proteins labeled with paramagnetic ions provides one way of achieving this. The project involves characterization of field induced orientation of model proteins including lectins that bind carbohydrate ligands.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。各向异性的NMR参数，如残余偶极耦合可以提供有价值的取向约束的结合态的碳水化合物与蛋白质相互作用的几何形状。然而，必须开发的方法，允许束缚态信息占主导地位的平均观察到的快速交换系统。用顺磁离子标记的蛋白质的场诱导取向提供了实现这一点的一种方式。该项目涉及表征场诱导的模式蛋白质，包括凝集素结合碳水化合物配体的方向。