It appears plausible that when the environment changes, protein functions are fine-tuned by the addition and/or deletion of functional motifs at the N-termini, or protein localizations are re-assigned by altering signal peptides or transporter activities.
As non-sense mutations probably change protein function, we category them as functional variants, and assign them the highest quantitative weight among others.
There were no nucleotide and/or codon substitutions predicted to change protein function that correlated with resistant and susceptible phenotypes.
Still, many of those mutations were predicted to change protein function.
We compared disease-associated single point mutations (nsSNPs) predicted to change protein function with those of unknown disease-association.
This is because, even where they change the amino acid sequence of a protein, not all genetic variants change protein function or cause disease.
These findings are consistent with H2O2 effects being mediated through the production of RLS, which are well known to modify proteins and change protein function.
The first and more intriguing is that SNPs being classified as deleterious are perhaps more likely to change protein function but not necessarily in a selectively negative way.
Importantly, considering that missense mutations do not necessarily change protein function as severely as nonsense or frameshift mutations, we primarily focused on base changes resulting in premature stop codons and indels within coding exons.
