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Phys Rev Lett. 2002 Nov 11;89(20):208101. Epub 2002 Oct 24.

Lack of self-averaging in neutral evolution of proteins.

Author information

1
Centro de Astrobiología (INTA-CSIC), 28850 Torrejon de Ardoz, Spain.

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.

PMID:
12443510
DOI:
10.1103/PhysRevLett.89.208101
[Indexed for MEDLINE]

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