Physics – Condensed Matter
Scientific paper
2002-09-19
Phys. Rev. Lett. 89, 208101 (2002)
Physics
Condensed Matter
4 pages, 2 figures
Scientific paper
10.1103/PhysRevLett.89.208101
We simulate neutral evolution of proteins imposing conservation of the thermodynamic stability of the native state in the framework of an effective model of folding thermodynamics. This procedure generates evolutionary trajectories in sequence space which share two universal features for all of the examined proteins. First, the number of neutral mutations fluctuates broadly from one sequence to another, leading to a non-Poissonian substitution process. Second, the number of neutral mutations displays strong correlations along the trajectory, thus causing the breakdown of self-averaging of the resulting evolutionary substitution process.
Bastolla Ugo
Porto Markus
Roman Eduardo H.
Vendruscolo Michele
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