# Speeding protein folding beyond the Go model: How a little frustration sometimes helps

Source: [Speeding protein folding beyond the Go model: How a little frustration sometimes helps](<https://www.sota2.com/research/paper/68fa1e307a2b558e293208a0>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-23T17:06:32.971Z

Authors: Steven S. Plotkin

Published: 2000-09-27T02:54:54.000Z

## Abstract

Perturbing a Go model towards 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 towards 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.

## Recorded benchmark results

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/cond-mat/0009413>)

[PDF](<https://arxiv.org/pdf/cond-mat/0009413.pdf>)