基于相对熵的蛋白质折叠、逆折叠方法的研究-流体力学专业论文.docxVIP

新方法的特例。第二部分对基于相对熵的蛋白质设计方法是否适用于不同结构 新方法的特例。第二部分对基于相对熵的蛋白质设计方法是否适用于不同结构 类型的蛋白质作了研究，分析了该方法对20种残基的预测成功率以及它们对 整体的预测成功率的影响，考察了二级结构中各残基的预测成功率以及它们对 整体的预测成功率的影响。结果证实了该方法普遍适用于四种结构类型的蛋白 质设计，也为基于相对熵的蛋白质设计方法的进一步发展做了准备；第三部分 是对基于相对熵的蛋白质折叠方法的扩展，提出了新的接触强度函数，使得该 方法更加合理，并提高了该方法的预测精度。 关键词蛋白质折叠：蛋白质逆折叠；相对熵；非格点模型；格点模型 II AbstractProteins，which Abstract Proteins，which are biologic macromolecules formed by amino acid residues， perform necessary and basic function in life．They participate in constructing the biologic structure and play the very important roles for the biologic function．The study on the relationship between structure and function of proteins ale hot in the field of molecule biology,since protein should lost its function once without their special native structure． The problem of protein folding is to study the principle how Can proteins have the special structures and the relation between their structures and biologic activity． The focus is how the amino acid residues carl fold proteins that have the particular structures，which is called the second genetic code．Protein folding is the key point of the relationship between genetic information and biologic function in the central dogma of molecular biology．The biologic molecular will be well understood if the protein folding problem will be solved． Protein inverse folding，which is also called嬲protein design，is to investigate how we can find the sequence from the given structure． There is a close relationship between protein design and protein folding． Understanding protein folding well is very helpful to solve the problem of protein design and vice versa． This work includes three parts：the first one is a generalized approach of a protein design method based on relative entropy，which Can increase the prediction precision for protein sequence and will be in favor of the study for protein design． The second one is a study on whether the protein design method based on relative entropy can be used in all proteins with different stru