Influence of interatomic interactions on the structure and stability of polypeptides and proteins

Several examples are cited to demonstrate how conformational‐energy calculations provide information about the manner in which interatomic interactions influence the structure and stability of polypeptides and proteins, and of intermolecular complexes involving these same species. These include the screw senses of α‐helical polyamino acids, helix–coil transition parameters, properties of β‐bends, and the structures of gramicidin S and of synthetic poly‐(tripeptide) models of collagen. In all of these calculations, the multiple‐minimum problem has been surmounted. A description is provided as to how the multiple‐minimum problem is being approached in calculations on globular proteins. These computational methods have also been applied to protein structure refinement and to the calculation of structures of homologous proteins and of enzyme–substrate complexes.