Cell functions can be understood as a complex and integrated network of intermolecular interactions. The flows of energy, matter, and information within and among cells are mediated by diverse arrays of proteins, nucleic acids, glycans, lipids, glycoproteins, and glycolipids. Notable, a key aspect of achieving detailed knowledge of molecular mechanisms and processes is the accurate determination of proteins' tridimensional structures, and despite the spectacular success of cutting-edge protein folding prediction methods, many critical questions remain unanswered. For this reason, our main interest focuses on understanding how an amino-acid sequence encodes its folding as well as how amino-acid substitutions and/or post-translational modifications might affect it.