Abstract
In this work, we present a brief and concise review about the main features of protein folding which is one of the central research questions at the interface of physics, molecular biology, and computational sciences. We describe the physical foundations of the protein folding phenomenon itself and how it arises as both a free energy minimization process combined with a hydrophobic collapse of the enzyme molten globule due to inter and intramolecular forces among amino acid residues themselves and water molecules. We cover briefly some basic statistical physics-based models to predict the thermodynamic properties of the protein folding transition. Then, we focus our attention on the implementation of computational algorithms designed to minimize energy functions in polypeptides.