  Protein folding is a phenomenon that has been studied for about 50 years and
still remains as an unsolved problem. The main feature of this process is that
it occurs as an all or none process, so a protein, can jump directly between
folded and unfolded states. It is proposed in this manuscript that the
cooperative phenomena associated to protein folding has its origin in the
synchronization oscillating phases of the instantaneously induced dipoles that
gives rise to the van der Waals London dispersion interaction. When the
oscillation of the induced dipoles is synchronized an enhanced interaction
regime is triggered and the protein enters a into a folding process. The
propagation of this regime throughout the molecular structure complete the
folding process. If a desynchronizing strong enough perturbation is introduced
at any component cooperative network the system enters in a weakened -- or even
a repulsive -- van der Waals dispersion interaction regime that propagate
itself throughout the structure, that triggers a phase transition that finally
unfolds the protein.
