Study of a model for the folding of a small protein
نویسندگان
چکیده
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 multidimensional replica exchange method with the widely used parallel tempering.
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