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Detalle de: Neutral Evolution of Model Proteins: Diffusion in Sequence Space and Overdispersion

Title Neutral Evolution of Model Proteins: Diffusion in Sequence Space and Overdispersion
Abstract

We stimulate the evolution of model protein sequences subject to mutations. A mutation is considered neutral if it conserves (1) the structure of the ground state, (2) its thermodynamic stability and (3) its kinetic accessibility. All other mutations are considered lethal and are rejected. We adopt a lattice model, amenable to a reliable solution of the protein folding problem. We prove the existence of extended neutral networks in sequence space-sequences can evolve until their similarity with the starting point is almost the same as for random sequences. Furthermore, we find that the rate of neutral mutations has a broad distribution in sequence space. Due to this fact, the substitution process is overdispersed (the ratio between variance and mean is larger than 1). This result is in contrast with the simplest model of neutral evolution, which assumes a Poisson process for substitutions, and in qualitative agreement with the biological data.

Apa Reference Bastolla, U., Roman, H. E., & Vendruscolo, M. (1999). Neutral Evolution of Model Proteins: Diffusion in Sequence Space and Overdispersion. Journal of Theoretical Biology, 200(1), 49–64. 10.1006/jtbi.1999.0975
Doi 10.1006/jtbi.1999.0975
Publication Date Sep 1999
Publication Type Article
Researcher Ugo Bastolla
Ontology Functional annotation, Function prediction, Structural bioinformatics, Molecular flexibility, Molecular evolution, Conservation Analysis, Evolutionary modelling, Ecological modelling, Sequence Alignment, Phylogenetic Analysis, Mutation Analysis and design, Network Biology, Structure-function relationship, Evolutionary rates, Microbial communities, Population dynamics
Research Groups Computational biology and Bioinformatics (CBM): from Proteins to Ecosystems
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