Evolution of Protein Interactions

摘要

A local optimisation method has been applied to the problem of folding and interaction between protein-like structures. These are composed of a randomly selected sequence of amino acids that are linked together to form linear polymers in three dimensions. The objective function chosen for optimisation is the potential energy given by a toy protein model. Convergence is reached as soon as the value for the objective function falls below a fixed valed given by an equilibrium temperature, T_(eq). Structures fold to minimise their objective function at a given rate, F_(rate), ranging from global optimisation of the whole structure to linear minimisation at every amino acid. The interaction between different structures is also modelled and optimised giving a whole range of local repulsion/attaction behaviours.