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).