Kinematics and thermodynamics of a folding heteropolymer.
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.
Fukugita
M
M
Yukawa Institute for Theoretical Physics, Kyoto University, Japan.
Lancaster
D
D
Mitchard
M G
MG
D017510:Protein Folding; D013816:Thermodynamics