许多蛋白质含有金属离子,金属离子对蛋白质发挥生物学功能起着很大的作用.金属离子与蛋白质的相互作用以及参与蛋白质功能调节的方式各种各样:有些金属离子高度专一性地与蛋白质紧密结合,对蛋白质发挥生物学功能起着关键性的作用;有些金属离子只是作为蛋白质发挥功能的辅助因子而瞬态地与蛋白质松散结合.本文简要介绍目前国际上用NMR方法研究抗磁金属离子和顺磁金属离子与蛋白质相互作用的进展,并具体介绍了NMR方法在钙调蛋白、锌指蛋白、朊病毒蛋白等金属离子蛋白研究上的应用.
Metal ions interact with protein using a great variety of mechanisms to regulate protein functions. Some metal ions bind tightly and specifically to proteins and markedly regulate protein function, while others interact loosely and nonspecifically with proteins and only act as cofactors for protein functioning. In this review, we describe nuclear magnetic resonance (NMR) techniques which are widely used to investigate inter-molecular interactions between proteins and diamagnetic/paramagnetic metal ions. Special emphasis is put on the NMR techniques the can be used to elucidate the structure and function of metalloproteins, including chemical shift mapping, paramagnetic NMR and backbone dynamics detection. Examples are given to illustrate how the NMR techniques can be used to map inter-molecular interaction between proteins (calmodulin, zinc fingers and prion proteins) and metal ions.