When those residues are connected to each other, they don't have COOH?
I read that in the spring, and managed to forget
N-terminal and C-terminal remain, but at the very ends of the protein
> Deamidation is a chemical reaction in which an amide functional group is removed from an organic compound. (Wikipedia says "removed", not "hydrolyzed")
I misenterpreted the Figure. The reaction starts in the top right corner.
> Deamidation is a post-translational modification in which an asparagine or glutamine residue of a protein loses an amide group and transforms into an aspartate/isoaspartate residue or a glutamate residue respectively.
But it does lose one nitrogen atom.
Since it is lost, we can say that the amide group is "removed" probably
> The process is non-enzymatic and goes faster at basic pH or if there is a glycine residue C-terminal-wise from the asparagine.
There must be a better formulation. (0:
> The process is non-enzymatic and goes faster at basic pH or if there is a glycine residue between the asparagine and the C-terminus.
> The process is non-enzymatic and goes faster at basic pH or if there is a glycine residue connected to the asparagine's C-terminal end.
I'm not sure if this is right, since the asparagine's residue would not have the C-terminal end if there's glycine connected to that.
> Deamidation proceeds much more quickly if the susceptible amino acid is followed by a small, flexible residue such as glycine whose low steric hindrance leaves the peptide group open for attack
Found it: the term is C-flanking
> Iso-Asp forms most easily in sequences where the side chain of the C-flanking amino acid is relatively small and hydrophilic, and is less likely to be formed where bulky or hydrophobic residues are in this position. The most favorable for Asp-isomerization C-flanking amino acids are Gly, Ser, and His
I hope I did not clutter the chat too much