Lack of Self-Averaging in Neutral Evolution of Proteins

Bastolla, U.; Porto, M.; Roman, H. E.; Vendruscolo, M.

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Lack of Self-Averaging in Neutral Evolution of Proteins

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Porto, M.
Max Planck Institute for the Physics of Complex Systems, Max Planck Society;

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Roman, H. E.
Max Planck Institute for the Physics of Complex Systems, Max Planck Society;

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Bastolla, U., Porto, M., Roman, H. E., & Vendruscolo, M. (2002). Lack of Self-Averaging in Neutral Evolution of Proteins. Physical Review Letters, 89(20): 208101. Retrieved from http://ojps.aip.org/getabs/servlet/GetabsServlet?prog=normal&id=PRLTAO000089000020208101000001&idtype=cvips&gifs=yes.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-369F-2

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.