title: Two-state models of protein folding kinetics.
abstract: The folding of some proteins appears to be a two-state kinetic process. A two-state kinetic model is justified if protein molecules rapidly equilibrate between different unfolded conformations prior to complete folding. Here I show that this rapid equilibration is a natural consequence of reasonable assumptions about reaction rate constants and folding thermodynamics.
authors.affiliation: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
authors.forename: R
authors.initials: R
authors.lastname: Zwanzig
mesh_terms: D007700:Kinetics; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics