Relaxation channels of two-vibron bound states in α-helix proteins
arXiv:physics/0310070 · doi:10.1103/PhysRevE.69.041906
Abstract
Relaxation channels for two-vibron bound states in an anharmonic alpha-helix protein are studied. It is pointed out that the relaxation originates in the interaction between the dressed anharmonic vibrons and the remaining phonons. This interaction is responsible for the occurrence of transitions between two-vibron eigenstates mediated by both phonon absorption and phonon emission. At biological temperature, it is shown that the relaxation rate does not significantly depends on the nature of the two-vibron state involved in the process. Therefore, the lifetime for both bound and free states is of the same order of magnitude and ranges between 0.1 and 1.0 ps for realistic parameters. By contrast, the relaxation channels strongly depend on the nature of the two-vibron states which is a consequence of the breather-like behavior of the two-vibron bound states.
arXiv commentoctobre 2003 - soumis Phys. Rev. E
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Cited by in corpus (7)
- Edge-localized states in quantum one-dimensional lattices
- Vibron-polaron in alpha-helices. I. Single-vibron states
- Biphonons in the Klein-Gordon lattice
- Vibron-polaron in alpha-helices. II. Two-vibron bound states
- Vibron-polaron critical localization in a finite size molecular nanowire
- Fast energy transfer mediated by multi-quanta bound states in a nonlinear quantum lattice
- Linear and non-linear infrared response of one-dimensional vibrational Holstein polarons in the anti-adiabatic limit: optical and acoustical phonon models