Hydrophobic models of protein folding and the thermodynamics of chain-boundary interactions

We review some results concerning the energetic and dynamical consequences of taking a generic hydrophobic model of a random polypeptide chain, where the effective hydrophobic interactions are represented by Hookean springs. Then we present a set of calculations on a microscopic model of hydrophobic interactions, investigating the behaviour of a hydrophobic chain in the vicinity of a hydrophobic boundary. We conclude with some speculations as to the thermodynamics of pre-biotic functions proteins may have discharged very early on in the evolutionary past.