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Study of a model for the folding of a small protein

Andrea Nobile·Federico Rapuano
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Abstract

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.

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Andrea Nobile, Federico Rapuano. 2005-11-30. Study of a model for the folding of a small protein. https://doi.org/10.1088/0953-8984%2F18%2F24%2F009

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