Conformational chaos and biomolecular instability in aqueous solution
Abstract
The glycine-rich tropoelastin tetrapeptide Ac-Gly-Leu-Gly-Gly-NMe has been modeled in aqueous solution by means of molecular dynamics simulations and the conformational motions have been characterized using nonlinear dynamics theory. Large amplitude fluctuations of the peptide backbone and H-bond patterns are detected. The end-to-end vector Ree undergoes anomalous diffusion with antipersistent fractional Brownian motion according to chaotic motions of molecules on fractal media. The vibrational picture of the intramolecular vectors shows a spatiotemporal self-similar disorder along the peptide chain on large scale observation demonstrating a high entropy state. The conformational chaos of the