Evolution of model proteins on a foldability landscape.
We model the evolution of simple lattice proteins as a random walk in a fitness landscape, where the fitness represents the ability of the protein to fold. At higher selective pressure, the evolutionary trajectories are confined to neutral networks where the native structure is conserved and the dynamics are non self-averaging and nonexponential. The optimizability of the corresponding native structure has a strong effect on the size of these neutral networks and thus on the nature of the evolutionary process.
Govindarajan
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Department of Chemistry, University of Michigan, Ann Arbor 48109-1055, USA.
Goldstein
R A
RA
D001704:Biopolymers / Q000737:chemistry; D019143:Evolution, Molecular; D008432:Mathematical Computing; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D001704:Biopolymers; D011506:Proteins