A dynamical approach to protein folding
Year: 2001
Authors: Torcini A., Livi R., Politi A.
Autors Affiliation: Univ Roma La Sapienza, Dipartimento di Fisica, Università “La Sapienza”, Piazzale A. Moro 2, 00185 Roma, Italy;
INFM, UdR Firenze, Largo E. Fermi 2, 50125 Firenze, Italy;
Dipartimento di Fisica, Università di Firenze, Largo E. Fermi 2, 50125 Firenze, Italy;
Istituto Nazionale di Ottica Applicata, Largo E. Fermi 6, 50125 Firenze, Italy
Abstract: In this paper we show that a dynamical description of the protein folding process provides an effective representation of equilibrium properties and it allows for a direct investigation of the mechanisms ruling the approach towards the native configuration. The results reported in this paper have been obtained for a two-dimensional toy-model of aminoacid sequences, whose native configurations were previously determined by Monte Carlo techniques. The somewhat controversial scenario emerging from the comparison among different thermodynamical indicators is definitely better resolved with the help of a truly dynamical description. In particular, we are able to identify the metastable states visited during the folding process by monitoring the temporal evolution of the ’long-range’ potential energy. Moreover, the resulting dynamical scenario is consistent with the picture arising from a reconstruction of the energy landscape in the vicinity of the global minimum. This suggests that the introduction of efficient ’static’ indicators too should properly account for the complex ’orography’ of the landscape.
Journal/Review: JOURNAL OF BIOLOGICAL PHYSICS
Volume: 27 (2-3) Pages from: 181 to: 203
KeyWords: dynamical simulations; off lattice models; proteinsDOI: 10.1023/A:1013104123892Citations: 19data from “WEB OF SCIENCE” (of Thomson Reuters) are update at: 2024-11-17References taken from IsiWeb of Knowledge: (subscribers only)Connecting to view paper tab on IsiWeb: Click hereConnecting to view citations from IsiWeb: Click here