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.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004058:Diffusion; D006860:Hydrogen Bonding; D007700:Kinetics; D008956:Models, Chemical; D009211:Myoglobin; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship
D009211:Myoglobin