Dynamical protein interaction pathways: A molecular root to diseases

We propose a complex dynamical model to mimic the protein-protein interaction. The signalling pathways that activate the proteins enact the intracellular functions are modelled by random and complimentary linking. The molecular roots of diseases are illuminated on the grounds of protein misfolding. Specifically, amy-loid fibrillated states are emphasized that are analogous to the coalescence of ordered and disordered dynamics. Also, a β− pleated sheet can be inferred from the model reflected as an anti-phase synchronized state. Note that the coupling strength is equivalent to the electromagnetic forces of the individual molecules. Critical clustering coupling strength has been analytically derived. Statistical techniques are imposed to impart an energy perspective of the model. We found that the relaxation time of the model plays a vital role in protein folding. We quote that ‘The quicker the folding, the lesser the entropy’. We validate the model using pathological data of breast carcinoma obtained from https://proteinatlas.org.