How much spatial change can amino acids of protein's active site withstand before being unable to perform protein's function?
We can, for example, compare X-ray or NMR structure of protein with modified structures of the same protein and conclude that the modified protein still has the same function because amino acids of the active site haven't changed their place, or we might conclude that, most probably, modified protein will lose function since amino acids of its active site have "moved" too much.
Is there a reference to how large this "too much" can be before protein loses function?
Thanks :)
This depends on the protein. Some proteins could lose function by just mutating a single residue, whereas, others can tolerate very many mutations, and can still carry out their function. So there is no general rule of thumb. It depends on individual proteins.
Hope this helps!
All the best,
Manjunatha
In order to answer the question following idea would help.
Protein structural changes caused by several reason can be classified and statistical analyses can help us to identify how much each of that changes can influence the function of proteins. It is obvious that we should started to collect a data of mutant proteins.
As mr Kogenaru said (above) it depends on the protein. Also on whic residue is replaced and how similar is the new residue, Changing valine to isoleucine will not bring as many changes as changing valine to proline for example.
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