摘要
为了克服双重蒙特卡罗方法用于较大分子体系及非格子模型的困难,提出了一个基于相对熵的蛋白质设计的简单方法.利用非格子模型,以16个处于天然稳定态的真实蛋白质为目标结构进行测试,成功率可达75.9％.与其他利用Monte Carlo方法搜索序列空间的方法相比,该方法更为快速有效,在很大程度上节省了对序列空间的搜索.
In order to overcome the difficulty of applying dual Monte Carlo method to the bigger molecule system and off-lattice model, a simple new method of protein design based on relative entropy is proposed. This method completely based on the principles of Physics adopts the off-lattice model and takes 16 real protein in the natural and stable state as the target structure to test and design, of which the success rate can reach 75.9%. As compared with other studies employing the sequence space Monte Carlo technique, this method is more speedy and effective, and saves the time, to great extent, of searching sequence space, which can be seen as the simplification and improvement of the previous works of the same kind.
出处
《北京工业大学学报》
CAS
CSCD
北大核心
2004年第1期106-109,共4页
Journal of Beijing University of Technology
基金
国家自然科学基金资助项目(10174005)
北京市自然科学基金资助项目(5032002).
关键词
蛋白质设计
蛋白质逆折叠
相对熵
protein design
inverse protein folding
relative entropy
