NMR OF PROTEIN-CARBOHYDRATE INTERACTIONS USING FIELD-INDUCED ALIGNMENT

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。各向异性的核磁共振参数，如残留的偶极偶联，可以为与蛋白质相互作用的碳水化合物的束缚态几何结构提供有价值的定向约束。然而，必须开发允许束缚状态信息主导在快速交换系统中观察到的平均值的方法。用顺磁离子标记的蛋白质的场诱导定向提供了一种实现这一点的方法。该项目涉及对模型蛋白质的场诱导定向的表征，包括结合碳水化合物配体的凝集素。

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.