Prediction of Protein-Folding Mechanism
	Munoz and Eaton computed folding rates by solving the diffusion equation of motion on the one-dimensional free-energy profiles that result from projection of the full free-energy landscape onto a reaction coordinate corresponding to the number of ordered residues. (a)shows the accuracy of their prediction by plotting computed folding rates (kcalc ) against experimentally measured rates (kexp). To predict folding transition state structure, the lowest free energy paths to the native state can be identified. For example, a beta-hairpin (b) has two possible paths to the native state, beginning at the hairpin (pathway 1) or at the free ends (pathway 2; ordered residues only are indicated; L is loop length). (c) shows that the transition state for both pathways consists of configurations with two of the residues ordered. The Table gives the contributions to the free energy of each configuration (total free energy is the sum of the first three columns) [Next]