Epistatic interactions modulate the evolution of mammalian mitochondrial respiratory complex components
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* Corresponding author: Luísa Azevedo lazevedo@ipatimup.pt
- Equal contributors
1 IPATIMUP-Institute of Molecular Pathology and Immunology of the University of Porto, Porto, Portugal
2 Faculty of Sciences of the University of Porto, Porto, Portugal
BMC Genomics 2009, 10:266 doi:10.1186/1471-2164-10-266
Published: 13 June 2009Additional files
Additional file 1:
Candidate compensatory residues for human deleterious mutations. This table provides all the possible compensatory sites for three human deleterious mutations found in non-human mammals.
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Additional file 2:
Quality evaluation of the modeled structures of human mitochondrial proteins. This figure presents the evaluation of model quality for the predicted 3D structures of human COI/COIII (A), CYB (B) and CYT1 (C) both overall (left) and locally (right) as estimated in ProSA-web. Both modeled structures showed z score values (black dots) that lie within the cloud, representing experimentally determined features of native proteins by X-ray and NMR analysis. Energy plots show a smooth fluctuation with overall negative energy of residue stretches (green lines) demonstrating that the predicted 3D structures show minimal deviations from normal energy values.
Format: TIFF Size: 215KB Download file
Additional file 3:
Consensus phylogeny of primate lineages. The figure shows the MrBayes consensus tree illustrating primate topology (A), the marginal density of posterior distribution of likelihood (LnL) for first and second MrBayes runs (B) and Tracer statistical results for tree likelihood, TL (tree length) and alpha in first and second run of MrBayes (C).
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