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, 5687-5694 [10.1088/0953-8984/18/24/009].
Citazione: | Rapuano, F., & Nobile, A. (2006). Study of a model for the folding of a small protein. JOURNAL OF PHYSICS. CONDENSED MATTER, 18, 5687-5694 [10.1088/0953-8984/18/24/009]. | |
Tipo: | Articolo in rivista - Articolo scientifico | |
Carattere della pubblicazione: | Scientifica | |
Titolo: | Study of a model for the folding of a small protein | |
Autori: | Rapuano, F; Nobile, A | |
Autori: | ||
Data di pubblicazione: | 2006 | |
Lingua: | English | |
Rivista: | JOURNAL OF PHYSICS. CONDENSED MATTER | |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1088/0953-8984/18/24/009 | |
Appare nelle tipologie: | 01 - Articolo su rivista |