Biology Direct, Год журнала: 2025, Номер 20(1)

Опубликована: Апрель 3, 2025

Protein folding remains a fundamental challenge in molecular biology, particularly understanding how polypeptide chains transition from denatured states to their functional conformations. Here we analyze the mechanisms of engineered metamorphic proteins B4 and Sb3, which share highly similar sequences but adopt distinct topologies. Kinetic analyses revealed that follows two-state mechanism, whereas Sb3 involves formation an intermediate species. We further explore role topology commitment using mutant Sb4, can populate both By analyzing unfolding behaviors under varying experimental conditions, our findings suggest dictates at early stage. These results demonstrate landscapes are primarily shaped by final native structures rather than sequence composition.

Язык: Английский