未配对电子与蛋白质分子自旋核的作用能提供丰富的长程结构信息,这些顺磁信息通常可用顺磁弛豫增强、赝接触位移和残余偶极耦合描述,其中赝接触位移包含生物大分子内重要的距离和角度信息。稀土离子具有相似的配位化学性质和不同的顺磁物理特性,而大多稀土离子具有磁各向异性,在与大分子作用过程中会产生赝接触位移。由于大多数蛋白质没有顺磁中心,获得这些顺磁信息需要通过定点选择标记蛋白质来实现。该文旨在对近年来蛋白质顺磁标记的方法和进展进行介绍,在顺磁标记基础上阐述赝接触位移在结构生物学中的应用。
The interactions between unpaired electrons and nuclear spins in proteins, usually represented in paramagnetic relaxation enhancement (PRE), pseudocontact shift (PCS) and residual dipolar couplings (RDC), provide rich sources of structural restraints. These paramagnetic effects are valuable in structure determination of protein and protein-ligand complex as well as in elucidation of protein dynamics. Because most proteins do not have paramagnetic centers, generation of paramagnetic restraints usually relies on site-specific labeling of proteins with paramagnetic ions. In this paper, efforts towards paramagnetic labeling of proteins, especially with lanthanide ions, are summarized, and PCS, as a powerful NMR spectroscopic tool for structural biology, is discussed.