Abstract

The potential energy surface of any system determines all the observable thermodynamic, kinetic and structural properties that involve a single electronic state. Addressing these properties directly in terms of energy landscapes has provided new insight in a wide range of apparently disparate fields. In particular, the non-random seaches that lead to protein folding, self-assembly, crystallisation, and magic numbers in molecular beams are probably all encoded within the structure of the potential energy surface. Examples will be illustrated for atomic and molecular clusters, peptides and small proteins, bulk matter, and a simple model of a virus capsid. New methods have been derived to calculate properties such as heat capacities and rate constants in terms of stationary points of the potential energy surface (minima and transition states). These tools enable us to tackle time and length scales that are inaccessible to conventional simulations. Results will be discussed for folding of met-enkephalin, the GB1 peptide, the villin headpiece subdomain, coarse-grained models of protein L and protein G, and misfolding of a coiled-coil trimer.