首页> 外文期刊>The European physical journal, B. Condensed matter physics >Long-range interactions in α-helical proteins with interspine coupling: Modulational instability and exact soliton solutions
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Long-range interactions in α-helical proteins with interspine coupling: Modulational instability and exact soliton solutions

机译:α-螺旋蛋白与脊柱间偶联的远距离相互作用:调制不稳定性和精确孤子解

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The dynamics of α-helical proteins with interspine coupling by taking into account long-range dipole-dipole interactions and some additional higher order molecular excitations is studied. The model Hamiltonian is transformed into a set of three classical lattice equations, which are further reduced in the multiple scales analysis to a set of three coupled nonlinear Schr?dinger (3-CNLS) equations. The linear stability analysis of continuous wave solutions of these 3-CNLS equations is performed and it reveals that the modulational instability (MI) gain is deeply influenced by the long-range interactions (LRI) parameter. Some classes of exact traveling wave solutions are constructed via the solutions of a ?4 model through the F-expansion method and representative wave structures are graphically displayed including localized and periodic solutions. In order to confirm the analytical approach, the numerical experiments show that the solitons are stable at 70 ps. These solitons, exhibited in the model, are a possible carrier of bio-energy transport in the protein molecules.
机译:通过考虑长距离偶极-偶极相互作用和一些其他更高阶的分子激发,研究了具有脊柱间耦合的α-螺旋蛋白的动力学。哈密​​顿量模型被转换为一组三个经典晶格方程组,在多尺度分析中将其进一步简化为一组三个耦合的非线性薛定er(3-CNLS)方程组。对这些3-CNLS方程的连续波解进行了线性稳定性分析,结果表明,调制不稳定性(MI)增益受远程相互作用(LRI)参数的影响很大。通过F展开法,通过?4模型的解,构造出某些类别的精确行波解,并以图形方式显示包括局部解和周期解在内的代表性波结构。为了确定分析方法,数值实验表明孤子在70 ps时稳定。模型中显示的这些孤子是蛋白质分子中生物能量传输的可能载体。

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