Come on Crash, thats clearly not true! Just look at your figure, a change of 1 base pair probably won't be a problem provided that it is the third base of the codon, but even a 1 bp change in the 1st or 2nd base will almost always produce a non-synonymous substitution.
There's a fair number of amino acids that have codons with two or even three differing bases. But you're right that that isn't most of them. And for most of them, the first codon nucelotide has to be the same.
But for most of them, the second and third can be changed. (Maybe you missed that some of them are listed twice?) I would offer that 2 out of 3 is large enough to be described as "probable."
70% of residues may well survive changing and allow a protein to function, although a reference would be nice to know exactly what research you are drawing from
Fair enough:
CB150: Functional genetic sequences changing
quote:
The analogy with language is flawed. Proteins are far more flexible. They can differ greatly in their sequence similarity, even 70-80% or more, and still have the same function.
The bibliography is at the bottom; the page does not make it clear which reference supports which claim, specifically.
but I doubt that if you changed 70% of the hydrophilic residues in a protein to hydrophobic residues you would get a functioning protein.
That may be. The page does not say.
Perhaps I overstated my claim. Nonetheless it's fairly clear that there is much resistance to mutation in the protein generation mechanism.