I am hoping that maybe you can guide me a little.
We both know that if one amino acid in the primary sequence of a protein
is deleted or changed, that that can potentially alter the proteins folded
shape which in turn can affect the protein's ability to execute its
specific function (eg sickle cell anemia).
It is my understanding that not all proteins lose their original function
when an amino acid is deleted or changed and that there exists studies
which show that renatured chains sometimes lead to fragmented structures
which through noncovalent forces recombine to create active structures
without lose of activity of the original parent protein.
Do you know of any articles or discussion on the different
activities that arise from renatured proteins with slightly changed
primary sequence?
Please, any response you can give me will be greatly appreciated.
Sincerely, Erich J. Ruth
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