Origins of globular structure in proteins

Abstract

Thermodynamic incompatibility of polymers in a common solvent is possibly a driving force for formation and evolution of globular protein structures. Folding of polypeptide chains leads to a decrease in both excluded volume of molecules and chemical differences between surfaces of globular molecules with chemical information hidden in the hydrophobic interior. Folding of polypeptide chains results in ‘molecular or thermodynamic mimicry' of globular proteins and in at least more than 10‐fold higher phase separation threshold values of mixed protein solutions compared to those of classical polymers. Unusually high co‐solubility might be necessary for efficient biological functioning of proteins, e.g. enzymes, enzyme inhibitors, etc.