beta_helix Staff Lv 1
You might be wondering how such a puzzle could be useful.
As many of you noticed during CASP10 when using the alignment tool, certain regions of the target sequence aligned very well (across all the different templates).
For example: perhaps all the templates had a helix when threading residues 1-30 for a particular target, but after residue 31 all the templates had very different topologies.
This is where freezing the N-terminal helix might be useful. In cases where the homology to known solved templates is very strong, we might want to use that exact structure and not let Rosetta wiggle it out of that conformation… instead letting you focus on the other regions.
To an extend we've tried using constraints for this, but often constraints make folding a lot more difficult. We'd like to see how you do with frozen regions.
Good luck and have fun… at least you don't need any secondary structure predictions!