Three-body Interactions Improve the Prediction of Rate and Mechanism in   Protein Folding Models
  Here we study the effects of many-body interactions on rate and mechanism in protein folding, using the results of molecular dynamics simulations on numerous coarse-grained C-alpha-model single-domain proteins. After adding three-body interactions explicitly as a perturbation to a Go-like Hamiltonian with native pair-wise interactions only, we have found 1) a significantly increased correlation with experimental phi-values and folding rates, 2) a stronger correlation of folding rate with contact order, matching the experimental range in rates when the fraction of three-body energy in the native state is ~ 20%, and 3) a considerably larger amount of 3-body energy present in Chymotripsin inhibitor than other proteins studied. 
M. R. Ejtehadi (1 and 2), S. P. Avall (1) and S. S. Plotkin (1) ((1)   Univ. of British Columbia, Canada, (2) Sharif Univ. o...