Open AccessTwo-state models of protein folding kinetics
Author(s) -
Robert Zwanzig
Publication year - 1997
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.94.1.148
Subject(s) - protein folding , folding (dsp implementation) , downhill folding , kinetics , reaction rate constant , thermodynamics , chemistry , kinetic energy , folding funnel , phi value analysis , lattice protein , physics , biochemistry , classical mechanics , electrical engineering , engineering
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.