The beginning construction features a terbium binding website from a beforehand designed coiled coil protein. The binding helices are held in place with sturdy constraints, as are the sidechains that bind the terbium ion. Nevertheless, the remainder of the protein must be folded and redesigned in order that the three symmetric copies will assemble accurately. The monomer subunit ought to have a robust core of hydrophobic residues. In comparison with the unique coiled coil, we expect this may give us elevated folding stability and higher binding.

This puzzle allows AlphaFold predictions for the monomer subunit of your design, so you’ll be able to add your answer for AlphaFold utilizing the AlphaFold prediction device. AlphaFold will predict the construction of your monomer subunit solely (i.e. within the unbound state, within the absence of different symmetric copies). When you load this prediction, then Foldit will try and align the prediction together with your answer. When you proceed working off of the AlphaFold prediction, you might must make changes on the interface the place the monomer subunit interacts with symmetric copies. The Buried Unsats Goal will incur a penalty for buried polar atoms that may’t make H-bonds. See the puzzle feedback for Goal particulars.