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].

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.
Articolo in rivista - Articolo scientifico
Scientifica
protein folding, parallel tempering
English
5687
5694
8
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].
Rapuano, F; Nobile, A
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/10281/4545
Citazioni
  • Scopus 0
  • ???jsp.display-item.citation.isi??? 0
Social impact