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Two-vibron bound states in α-helix proteins:: The interplay between the intramolecular anharmonicity and the strong vibron-phonon coupling -: art. no. 021909

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PHYSICAL REVIEW E
卷 68, 期 2, 页码 -

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AMER PHYSICAL SOC
DOI: 10.1103/PhysRevE.68.021909

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The influence of the intramolecular anharmonicity and the strong vibron-phonon coupling on the two-vibron dynamics in an alpha-helix protein is studied within a modified Davydov model. The intramolecular anharmonicity of each amide-I vibration is considered, and the vibron dynamics is described according to the small polaron approach. A unitary transformation is performed to remove the intramolecular anharmonicity, and a modified Lang-Firsov transformation is applied to renormalize the vibron-phonon interaction. Then a mean field procedure is realized to obtain the dressed anharmonic vibron Hamiltonian. It is shown that the anharmonicity modifies the vibron-phonon interaction, which results in an enhancement of the dressing effect. In addition, both the anharmonicity and the dressing favor the occurrence of two different bound states whose properties strongly depend on the interplay between the anharmonicity and the dressing. This dependence was summarized in a phase diagram which characterizes the number and the nature of the bound states as a function of the relevant parameters of the problem. For a significant anharmonicity, the low-frequency bound states describe two vibrons trapped onto the same amide-I vibration, whereas the high-frequency bound states refer to the trapping of the two vibrons onto nearest neighbor amide-I vibrations.

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