Estimates for the Potential Accuracy Required in Realistic Protein Folding Simulations and Structure Recognition Experiments

Background: We have recently addressed the problem of potential accuracy required for protein folding simulations using a combination of theoretical considerations and lattice model simulations. In the present study we combine the previously developed theoretical formalism with the law of corresponding states recently proposed by Onuchic, Wolynes and collaborators and obtain estimates for the potential accuracy required for computational studies of a small helical protein. Results: Our estimates suggest that effective energies of interaction between amino acid residues could be measured with an error around \Sigma330 cal/mol for a resulting inaccurate potential still appropriate for structure recognition experiments, where the native conformation must remain the global energy minimum. For an ab initio folding simulation, where the energy of the native conformation must be sufficient to balance the entropy of the denatured state at a temperature at which the dynamics of the system is ..