title: Kinematics and thermodynamics of a folding heteropolymer.
abstract: In order to elucidate the folding dynamics of protein, we have carried out numerical simulations of a heteropolymer model of self-interacting random chains. We find that folding propensity depends strongly on sequence and that both folding and nonfolding sequences exist. Furthermore we show that folding is a two-step process: the transition from coil state to unique folded state takes place through a globule phase. In addition to the continuous coil-globule transition, there exists an abrupt transition that separates the unique folded state from the globule state and ensures the stability of the native state.
authors.affiliation: Yukawa Institute for Theoretical Physics, Kyoto University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Fukugita
authors.forename: D
authors.initials: D
authors.lastname: Lancaster
authors.forename: M G
authors.initials: MG
authors.lastname: Mitchard
mesh_terms: D017510:Protein Folding; D013816:Thermodynamics