Navigation and analysis of the energy landscape of small proteins using the activation-relaxation technique.
The resolution of the protein folding problem has been tied to the development of a detailed understanding of the configurational energy or of the free energy landscape associated with these molecules. Using the activation-relaxation technique and a simplified energy model, we present here a detailed analysis of the energy landscape of 16-residue peptide that folds into a beta-hairpin. Our results support the concept of an energy landscape with an effective topology consistent with a scale-free network.
Mousseau
Normand
N
Département de Physique and Regroupement Québécois sur les Matériaux de Pointe, Université de Montréal, Case Postale 6128, Succursale Centre-Ville, Montréal, Québec, H3C 3J7, Canada.
Derreumaux
P
P
Gilbert
G
G
D001703:Biophysics / Q000379:methods*; D003198:Computer Simulation; D019277:Entropy; D008962:Models, Theoretical; D008968:Molecular Conformation; D009010:Monte Carlo Method; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D010455:Peptides; D011506:Proteins