  Different models such as diffusion-collision and nucleation-condensation have
been used to unravel how secondary and tertiary structures form during protein
folding. However, a simple mechanism based on physical principles that provide
an accurate description of kinetics and thermodynamics for such phenomena has
not yet been identified. This study introduces the hypothesis that the
synchronization of the peptide plane oscillatory movements throughout the
backbone must also play a key role in the folding mechanism. Based on that, we
draw a parallel between the folding process and the dynamics for a network of
coupled oscillators described by the Kuramoto model. The amino acid coupling
may explain the mean-field character of the force that propels an amino acid
sequence into a structure through self-organization. Thus, the pattern of
synchronized cluster formation and growing helps to solve the Levinthal's
paradox.Synchronization may also help us to understand the success of homology
structural modeling, allosteric effect, and the mechanism responsible for the
recognition of odorants by olfactory receptors.
