Speeding protein folding beyond the Go model: How a little frustration sometimes helps
Disordered Systems and Neural Networks
2007-05-23 v1 Soft Condensed Matter
Statistical Mechanics
q-bio
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.
Cite
@article{arxiv.cond-mat/0009413,
title = {Speeding protein folding beyond the Go model: How a little frustration sometimes helps},
author = {Steven S. Plotkin},
journal= {arXiv preprint arXiv:cond-mat/0009413},
year = {2007}
}
Comments
12 pages, 5 figures, 1 table. submitted to Proteins: Struct. Funct. Genet