Choice of sequence homologs included in multiple sequence alignments has a dramatic impact on evolutionary conservation analysis
The analysis of sequence conservation patterns has been widely utilized to identify functionally important (catalytic and ligand-binding) protein residues for over a half-century. Despite decades of development, on average state-of-the-art non-template-based functional residue prediction methods must predict ∼25% of a protein’s total residues to correctly identify half of the protein’s functional site residues. The overwhelming proportion of false positives results in reported “F-Scores” of ∼0.3. We investigated the limits of current approaches, focusing on the so-far neglected impact of the specific choice of homologs included in multiple sequence alignments (MSAs).See it on Scoop.it, via Viruses, Immunology & Bioinformatics from Virology.uvic.ca
Choice of sequence homologs included in multiple sequence alignments has a dramatic impact on evolutionary conservation analysis
Source: Viral Bioinformatics
