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

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dc.creatorPlotkin, Steven S.
dc.date2000-09-27
dc.date.accessioned2026-07-07T02:38:51Z
dc.date.available2026-07-07T02:38:51Z
dc.descriptionPerturbing 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.
dc.description12 pages, 5 figures, 1 table. submitted to Proteins: Struct. Funct. Genet
dc.identifierhttps://arxiv.org/abs/cond-mat/0009413
dc.identifierhttp://arxiv.org/abs/cond-mat/0009413
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/16832
dc.subjectDisordered Systems and Neural Networks
dc.subjectSoft Condensed Matter
dc.subjectStatistical Mechanics
dc.subjectQuantitative Biology
dc.titleSpeeding protein folding beyond the Go model: How a little frustration sometimes helps
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