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计算机辅助蛋白质分子理性设计在解决化学及生物学重要问题中被证实十分有效。在NOR本身三维结构未知的情况下通过计算机分子模拟,使用肌红蛋白(Mb)作为蛋白质分子模型,设计了结构功能型一氧化氮还原酶(NOR),所设计的NOR蛋白质模型——FeBMb一年后被天然NOR的晶体结构所证实。本文综述了设计FeBMb,I107E FeBMb以及FeBMb(-His)的研究过程及其设计合理性,评述了通过使用计算机分子模拟,获得Mb处于双组氨酸配位的非天然状态的原子层次结构信息,而这些信息很难通过实验方法来获得。计算机辅助蛋白质分子理性设计的广泛应用将会为生物体系提供更深刻的内涵。
Computer-Aided Protein Molecular Rational Design has proven to be very effective in solving important chemical and biological problems. In the case of unknown three-dimensional structure of NOR itself, structural functional nitric oxide reductase (NOR) was designed by computer molecular simulation using myoglobin (Mb) as a protein molecular model. The designed NOR protein model, FeBMb Years later confirmed by the natural NOR crystal structure. In this paper, the research process and design rationality of designing FeBMb, I107E FeBMb and FeBMb (-His) are reviewed. The atomic hierarchical structure of Mb in the non-natural state of histidine coordination is obtained by using computer molecular simulation. This information is difficult to obtain by experimental methods. The widespread application of computer-aided protein molecular rational design will provide biological systems with more profound connotations.