Speeding protein folding beyond the G(o) model: how a little frustration sometimes helps
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Updated: Oct 3, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
1Department of Physics, University of California, San Diego, California, USA. steve@physics.ubc.ca
Abstract:
By perturbing a G(o) model toward a realistic protein Hamiltonian by adding non-native interactions, we find that the folding rate is in general enhanced as ruggedness is initially increased, as long as the protein is sufficiently large and flexible. Eventually, the rate drops rapidly toward zero when ruggedness significantly slows conformational transitions. Energy landscape arguments for thermodynamics and kinetics are coupled with a treatment of non-native collapse to elucidate this effect.
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