摘要
基于蛋白质二维HP非格模型和改进的模拟退火算法研究了长短程作用在蛋白质折叠过程中的作用。通过试验得出1ECD、2RNS、1PHT、1WBC等序列的折叠构型,并根据PDB中所提供的上述序列的结构信息,具体讨论了长程作用对蛋白质构型的影响,说明了:长程作用在三级结构的形成和稳定中,位于诸多影响因素的首位。
Based on the protein 2-dimension HP off-lattice model and the improved simulated annealing algorithm, this paper discusses the respective roles of short- and long interactions in protein folding, the configurations of 1ECD ,2RNS, 1PHT, 1WBC are obtained, and with their structure information in the PDB, the influence of long-range interactions is discussed. The results show that for the folding and stability of proteins, long-range interactions are the main determinants.
出处
《计算机与应用化学》
CAS
CSCD
北大核心
2005年第10期832-836,共5页
Computers and Applied Chemistry
基金
国家自然科学基金资助项目(90103033)
关键词
长短程相互作用
蛋白质折叠
模拟退火算法
二维HP非格模型
long and short-range interactions, proteins folding, simulated annealing algorithm, 2-dimension HP off-lattice model