摘要
生物体系中金属离子在调节金属蛋白的结构和功能中发挥着至关重要的作用。本文综述了利用人工金属结合位点的理性设计来扩展蛋白质功能的研究进展,包括在蛋白分子内部通过探索潜在的金属结合位点、重新设计已有的金属结合位点,以及设计全新的金属结合位点的方法来设计人工金属结合位点;在蛋白分子表面进行设计,来获得结构及功能的转化、研究与纳米材料间的相互作用,以及进行蛋白质分子的自组装。这些研究极大地丰富了我们对金属蛋白结构与功能关系的认识。同时,也赋予了我们控制及利用感兴趣蛋白的能力。
Metal ions play crucial roles in mediating the structures and functions of metalloproteins in biological systems.This review summarized the progress of using rational design of artificial metal-binding sites to expand the functional diversity of proteins,which includes designing artificial metal-binding sites within protein scaffolds by exploring potential metal-binding sites,redesigning existing metal-binding sites,or designing new metal-binding sites,and on the protein surfaces to achieve structural and functional conversions,studying interactions with nanomaterials,or performing protein self-assembly.These progresses greatly enriched our knowledge of the structure-function relationships of metalloproteins,and also endowed us the ability to control and utilize a protein of interest.
出处
《化学进展》
SCIE
CAS
CSCD
北大核心
2010年第6期1203-1211,共9页
Progress in Chemistry
关键词
金属结合位点
分子设计
结构
功能
metal-binding sites
molecular design
structure
function
