Nonlinear Correlations of Protein Sequences and Symmetries of Their Structures

We investigate the nonlinear correlations of protein sequences by using the nonlinear prediction method developed in nonlinear dynamical theory. It is found that a lot of protein sequences show strong nonlinear correlations and have deterministic structures. Further investigations show that the strong nonlinear correlations of these protein sequences are due to the symmetries of their tertiary structures. Furthermore, the correlation lengths of the sequences are related to the degrees of the symmetries. These results support the duplication mechanism of protein evolution and also reveal one aspect how amino acid sequences encode their spatial structures.     

Nonlinear Dynamics Approach to the Correlation Analysis of Protein Sequences

To clarify the randomness of protein sequences,we make a detailed analysis of a set of typical protein sequences representing each fold by using the nonlinear prediction method developed in nonlinear dynamics theory.No deterministic structures are found in these protein sequences and this implies that they behave as random chains.We also explain the controversial results obtained in previous investigations.     

能量在蛋白质α-螺旋链中传输模型的稳定性分析

引入了一个新的模型来描述α螺旋蛋白质分子中3条单肽链的振动能量的贮存和传输,在该模型中考虑了链间的相互作用能量,并对该模型进行了稳定性分析,发现该模型存在非线性局域模,数值模拟的结果表明,该模型存在静止和运动的局域模型.     

激光—激光子相互作用蛋白质能量传输模型的数值模拟研究

引入了一个新的模型来描述蛋白质子中Ａｍｉｄｅ－Ⅰ振动能量的贮与传输。这种模型是在Ｄａｖｙｄｏｖ模型的基础上加以改进，引入激子的相互作用项。并用数值模拟的方法说明了该模型可以存在静止和运动的局域模式。