CAJ | 학술논문

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。
미배대전자여단백질분자자선핵적작용능제공봉부적장정결구신식，저사순자신식통상가용순자이예증강、안접촉위이화잔여우겁우합묘술，기중안접촉위이포함생물대분자내중요적거리화각도신식。희토리자구유상사적배위화학성질화불동적순자물리특성，이대다희토리자구유자각향이성，재여대분자작용과정중회산생안접촉위이。유우대다수단백질몰유순자중심，획득저사순자신식수요통과정점선택표기단백질래실현。해문지재대근년래단백질순자표기적방법화진전진행개소，재순자표기기출상천술안접촉위이재결구생물학중적응용。
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.