Protein Folding/Unfolding Phenomenon is originated by Synchronization/Desynchronization of Instantaneously Induced Oscillating Dipoles. A Hypothesis

TL;DR

This paper hypothesizes that protein folding and unfolding are driven by synchronization and desynchronization of oscillating dipoles, affecting van der Waals interactions and causing all-or-none folding transitions.

Contribution

It introduces a novel hypothesis linking protein folding to dipole oscillation synchronization, offering a new perspective on the underlying physical mechanism.

Findings

Proposes synchronization of dipoles as a key factor in folding.

Suggests desynchronization causes unfolding via phase transition.

Connects protein folding to oscillating dipole interactions.

Abstract

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.