1.
Proc Natl Acad Sci U S A
; 90(13): 6365-8, 1993 Jul 01.
Artículo
en Inglés
| MEDLINE
| ID: mdl-8327518
RESUMEN
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.