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Solitons on H-bonds in proteins

Francesco d'Ovidio·Henrik Bohr·Per-Anker Lindgaard
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Abstract

A model for soliton dynamics on a hydrogen-bond network in helical proteins is proposed. It employs in three dimensions the formalism of fully integrable Toda lattices which admits phonons as well as solitons along the hydrogen-bonds of the helices. A simulation of the three dimensional Toda lattice system shows that the solitons are spontaneously created and are stable and moving along the helix axis. A perturbation on one of the three H-bond lines forms solitons on the other H-bonds as well. The robust solitary wave may explain very long-lived modes in the frequency range of 100 cm$^{-1}$ which are found in recent X-ray laser experiments. The dynamics parameters of the Toda lattice are in accordance with the usual Lennard-Jones parameters used for realistic H-bond potentials in proteins.

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Francesco d'Ovidio, Henrik Bohr, Per-Anker Lindgaard. 2003-09-16. Solitons on H-bonds in proteins. https://doi.org/10.1088/0953-8984%2F15%2F18%2F304

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