Analysis of biomolecular chaos in aqueous solution

Abstract.

 The tropoelastin peptide CH₃CO-Gly-Leu-Gly-Gly-NHCH₃ has been modeled in aqueous solution by means of force-field molecular dynamics simulations and its motion characterized using nonlinear dynamics theory. The trajectory R(t) of the representative system point in configurational space has been considered. Fractional Brownian motion with anomalous diffusion is observed resulting from chaotic dynamics of molecules on fractal media. The chaos of the peptide is a consequence of nonlinear effects such as hydrodynamic interactions of the chain due to the poor solvent role of water. The viscous drag is pointed out and should be due to the percolation network of hydrogen-bonded water molecules. The method of reconstruction of the phase space using the embedding theorem is applied to the trajectory D _ee(t) of the peptide end-to-end distance. The existence of a low-dimensional chaotic attractor for dissipative systems has been demonstrated. The dynamical high-entropy state of the peptide in solution strengthens the transition-to-chaos mechanism for the elastin elasticity.