2.3. SARS-CoV-2 Nsp1 substitutions
SARS-CoV-2 Nsp1 mutations (substitutions, insertions, and deletions) were retrieved from the Glu-CoV database (http://cov-glue.cvr.gla.ac.uk/) [30]. The identified substitutions in the Nsp1 C-terminal (helix-turn-helix) were examined in the DynaMut [31] web server to determine their effects on protein stability. The effect of mutations in protein stability and the estimation of change in the folding free energy upon the mutation (ΔΔGDestablizing)[31,32] and vibrational entropy energy (ΔΔSVis) was predicted using the DynaMut tool[31]. MutaBind2 [33] was used to evaluate the effects of mutations on Nsp1-ribosome interactions. This server computed changes in binding affinity upon single mutations (ΔΔGBinding).