Dear all,

I am working on a project concerning Inverse folding Problem. I have a protein of interest which apparently mis-folds, after a certain age and cause aggregation.

The protein has 200 (approx) residues out of which 92 residues are conserved and functionally important. I have written a code which generate sequences restricting or fixing the conserved ones (46%) but allowing other residues to shuffle. Also, the composition stays as it is in the wild type.

If the sequences are modelled using current protein threading techniques , Is it likely that a particular sequence would adopt the same fold but still be structurally different? Please share your opinions.