ProtEvol
For a protein with known structure, the program ProtEvol performs two kinds of computation:
- It computes the mean-field model of protein evolution, which consists in the stationary amino acid distribution with independent sites that has minimum Kullback-Leibler
divergence with respect to a background distribution and that constraints the average stability of the native state of the protein against both unfolding and misfolding.
The background distribution and the selection parameter that enforces the desidered stability are optimized by maximum likelihood.
For each site of the protein with known structure, it outputs the site-specific stationary amino acid distribution and the exchangeability matrix
related to it through the Halpern-Bruno formula, with which phylogenetic inference can be performed. The global model needed for computing the
branch lengths is obtained by averaging the site-specific models.
Reference: Arenas M, Sánchez-Cobos A, Bastolla U. Maximum-Likelihood Phylogenetic Inference with Selection on Protein Folding Stability.
Mol Biol Evol. 2015 32:2195-207. [Pubmed]
- It simulates protein evolution subject to the constraint of selection on the folding stability of the native state of the
protein against both unfolding and misfolding. It implements three selection models:
- Neutral: Mutations are accepted if DeltaG smaller X*DeltaG(wild type), otherwise they are rejected.
- From the DeltaG of the mutant, the fitness is computed as f=1/(1+exp(DeltaG/kT)) and the acceptance probability is computed with Kimura's formula.
- Based on the mean-field evolutionary model computed at the previous point.
Reference: R. Méndez, M. Fritsche, M. Porto and U.Bastolla. Mutation bias favors protein folding stability in the evolution of small populations.
PLoS Comput Biol 6: e1000767 2010 [Pubmed]
- Instalación : Documentación incluida en el paquete.
- Licencia: Uso gratuito para fines educacionales y de investigación.
- Contactar con: ub@cbm.uam.es
- Descargar: Es necesario registrarse primero.