2026-07-072026-07-07http://salesiana.dossiersoluciones.com/handle/123456789/16832Perturbing 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.12 pages, 5 figures, 1 table. submitted to Proteins: Struct. Funct. GenetDisordered Systems and Neural NetworksSoft Condensed MatterStatistical MechanicsQuantitative Biologytext