A diffusion--collision--adhesion model for the kinetics of myoglobin refolding.

There are two distinct experimental and theoretical problems of protein folding: the thermodynamic issue of characterizing the folded state, and the kinetic question of the path between the unfolded and native states. Here we consider the second question and present a diffusion--collision--adhesion model for the folding of the alpha-helical protein myoglobin. In particular, we consider the fast refolding species of the unfolded state and ignore the slow transition between unfolded states that has been attributed to proline isomerization.