Protein folding and unfolding reactions are slowed down by free energy barriers that arise
when changes in enthalpy and entropy do not compensate for each other during the course
of the reaction. The nature of these free energy barriers is poorly understood. The common
assumption is that a single dominant barrier (> 3 kBT), describable in terms of a single
reaction coordinate, slows down the structural transition, which then becomes an all-or-none
transition. This assumption has allowed the empirical application of transition state theory …

Protein folding and unfolding reactions are slowed down by free energy barriers that arise
when changes in enthalpy and entropy do not compensate for each other during the course
of the reaction. The nature of these free energy barriers is poorly understood. The common
assumption is that a single dominant barrier (&gt; 3 k< sub> BT), describable in terms of a
single reaction coordinate, slows down the structural transition, which then becomes an all-
or-none transition. This assumption has allowed the empirical application of transition state …