Proteins are fundamental macromolecules for life, with a diversity of functions, like acting as channels through cellular walls, catalysers, DNA benders, etc. When it comes to these functions, what matters is the layout of the secondary branches, made up of each protein’s amino acids, such as alanine, glutamine, arginine, phenylalanine and tyrosine. These are stabilised mainly by weak interactions— such as hydrogen bonds, intramolecular interactions, and inter molecular dispersive forces,—between the backbone and the lateral chain of their amino acids.