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作 者:秦红珊[1] 孙凤兰[1] 王克起[1] 杨新岐[2]
机构地区:[1]天津大学理学院物理系,天津300072 [2]天津大学材料科学与工程学院,天津300072
出 处:《生物数学学报》2004年第2期238-244,共7页Journal of Biomathematics
基 金:国家自然科学基金科普项目(70120001)资助
摘 要:从蛋白质折叠成自由能最小的稳定结构类型为研究的出发点,为揭示蛋白质空间折叠的动力学本质,对非同源蛋白质数据库,以蛋白质序列的氨基酸频率和自协方差函数为特征矢量,求出表征特征矢量中各分量耦合作用与协同作用的协方差矩阵所对应的特征值.与Chou的方法相比,更全面地反映了蛋白质折叠密码的简并性、全局性和多意性,为定量表征折叠成不同结构类的蛋白质,提供了一种动力学参数分析方法.In order to investigate the properties of the protein folding patterns based on the concept that the protein sequences should be folded into one of the steady structure classes with the lowest free energy, the eigen-values and eigen-vectors of the covariance matrix by using the amino acid composition combing with the auto-covariance functions as the features are calculated for the non-homologous protein database used in here. It is found that the interaction (indicated by the eigen-values and eigen-vectors above) among the components of the amino acid composition and auto-covariance functions more effectively represents the folding properties of protein sequences. As comparing with the Chou's method, the suggested approach could more really reflect the degenerative, comprehensive and variegated natures of protein folding patterns. It provided a new method to quantitatively analyze the protein sequences folded into different four types of structures classes.
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