In the diffusion-collision model, the unfolding rates are given by the likelihood of secondary structural cluster dissociation. In this work, we introduce an unfolding rate calculation for proteins whose secondary structural elements are $\alpha$ helices, modeled from thermal escape over a barrier that arises from the free energy in buried hydrophobic residues. Our results are in good agreement with currently accepted values for the attempt rate.

• Received 13 June 2001

DOI:https://doi.org/10.1103/PhysRevE.64.052902