The thermodynamic origin of thermophilic ribozyme

bozyme become linked into a single transition in the folding of the thermophilic ribozyme. Therefore, the starting point, or reference nc state, for the transition to the native, functional thermophilic in ribozyme is significantly less structured. The shift in the reference th state, and the resulting increase in folding cooperativity, is likely bc due to the stabilization of selected native interactions that only M form in the ultimate transition. This mechanism of using a less th structured intermediate and increased cooperativity to achieve se higher functional stability for tertiary RNAs is fundamentally th different from that commonly proposed to explain the increased R stability of thermophilic proteins. tr