Study of a model for the folding of a small protein

We describe the results obtained from an improved model for protein folding. We find that a good agreement with the native structure of a 46 residue long, five-letter protein segment is obtained by carefully tuning the parameters of the self-avoiding energy. In particular we find an improved free-energy profile. We also compare the efficiency of the multidimensional replica exchange method with the widely used parallel tempering.