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Updated: Jul 15, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Three-body interactions improve the prediction of rate and mechanism in protein folding models
M R Ejtehadi1, S P Avall, S S Plotkin
1Department of Physics and Astronomy, University of British Columbia, Vancouver, BC, Canada V6T 1Z1. ejtehadi@physics.ubc.ca
Abstract:
Here we study the effects of many-body interactions on rate and mechanism in protein folding by using the results of molecular dynamics simulations on numerous coarse-grained Calpha-model single-domain proteins. After adding three-body interactions explicitly as a perturbation to a Gō-like Hamiltonian with native pairwise interactions only, we have found (i) a significantly increased correlation with experimental phi values and folding rates, (ii) 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 approximately 20%, and (iii) a considerably larger amount of three-body energy present in chymotripsin inhibitor than in the other proteins studied.
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