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. © 2006 IOP Publishing Ltd.
Rapuano, F., Nobile, A. (2006). Study of a model for the folding of a small protein. JOURNAL OF PHYSICS. CONDENSED MATTER, 18(24), 5687-5694 [10.1088/0953-8984/18/24/009].
Study of a model for the folding of a small protein
RAPUANO, FEDERICO;
2006
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. © 2006 IOP Publishing Ltd.
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