Compared to Synthetic Polymers, Proteins Are Awesome

This paper is written for undergraduate chemistry students who are introduced to the elegant biosynthesis and folding of proteins as compared to synthetic polymers. The uniqueness of proteins among other synthetic and biopolymers is discussed. Proteins are characterized by unique 3‐dimensional structures that are dictated by their 1‐dimensional amino acid sequences. The driving force of the 3‐d conformation lies in the tendency of hydrophobic residues to stay away from an aqueous environment. As a result of such hydrophobic forces, proteins are very compact. Conformational folding is much faster than the time needed for an exhaustive search of the global minimum energy. Additionally, conformational changes induced by environmental factors such as pH, temperature, or ligands are cooperative. Such cooperative folding is given by an example of hemoglobin binding to oxygen molecules. Polymer synthesis designed to mimic protein structures has given useful polymers with many practical applications.