title: Lack of self-averaging in neutral evolution of proteins.
abstract: 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.
authors.affiliation: Centro de Astrobiología (INTA-CSIC), 28850 Torrejon de Ardoz, Spain.
authors.forename: Ugo
authors.initials: U
authors.lastname: Bastolla
authors.forename: Markus
authors.initials: M
authors.lastname: Porto
authors.forename: H Eduardo
authors.initials: HE
authors.lastname: Roman
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
mesh_terms: D003574:Cytochrome c Group / Q000737:chemistry / Q000235:genetics; D019143:Evolution, Molecular; D008957:Models, Genetic; D009113:Muramidase / Q000737:chemistry / Q000235:genetics; D009154:Mutation; D009211:Myoglobin / Q000737:chemistry / Q000235:genetics; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics; D012416:Rubredoxins / Q000737:chemistry / Q000235:genetics; D013816:Thermodynamics
chemical_list: D003574:Cytochrome c Group; D009211:Myoglobin; D011506:Proteins; D012416:Rubredoxins; D012260:Ribonucleases; D009113:Muramidase