We have investigated an evolutionary algorithm for de novo all-atom folding of the bacterial ribosomal protein L20. We report results of two simulations that converge to near-native conformations of this 60-amino-acid, four-helix protein. We observe a steady increase of "native content" in both simulated ensembles and a large number of near-native conformations in their final populations. We argue that these structures represent a significant fraction of the low-energy metastable conformations, which characterize the folding funnel of this protein. These data validate our all-atom free-energy force field PFF01 for tertiary structure prediction of a previously inaccessible structural family of proteins. We also compare folding simulations of the evolutionary algorithm with the basin-hopping technique for the Trp-cage protein. We find that the evolutionary algorithm generates a dynamic memory in the simulated population, which leads to faster overall convergence. © 2006 by the Biophysical Society.
CITATION STYLE
Schug, A., & Wenzel, W. (2006). An evolutionary strategy for all-atom folding of the 60-amino-acid bacterial ribosomal protein L20. Biophysical Journal, 90(12), 4273–4280. https://doi.org/10.1529/biophysj.105.070409
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