Proteus: An algorithm for proposing stabilizing mutation pairs based on interactions observed in known protein 3D structures

Table 3 List of predicted mutations for the bacteriophage T4 lysozyme (PDB ID: 2LZM)

Mutations predicted by Proteus (left). Mutations with experimental evidence (right). R1: first amino acid residue from the template where the mutation pair was extracted; R2: second amino acid residue from the template where the mutation pair was extracted; ΔΔG: Gibbs free energy variation (ΔΔGp: predicted; ΔΔGe: experimental). The predicted mutations are available at http://proteus.dcc.ufmg.br/result/id/SYLX52 (details were included in the supplementary material: Tables S6 and S11). ^a ΔΔG_e was multiplied for − 1 because of ProTherm uses a different ΔΔG definition when compared to MAESTRO. ProTherm considers positive values of ΔΔG as stabilizing, while MAESTRO considers negative values of ΔΔG as stabilizing. While one of them uses ΔG = G_folded-G_unfolded, the other uses ΔG = G_unfolded-G_folded

ISSN: 1471-2105