who is this "advanced player" refereed in article? He was picking best solutions (ie 200 out of 100`000) :)

Thank you very much for the PDF! :)

In the SI I see the names of several players from the early days of Foldit who are no longer actively participating. I hope where possible they can be contacted so that they can see their contribution recognized: some may even be encouraged to return as a result.

I was the advanced Foldit player referenced in the paper as well as a first author on the paper. I primarily used the standalone version of Foldit when working on and evaluating structures and thus didn't have much presence in game. We are continually impressed with the structures produced by players, and it was a pleasure to review and test them in lab. We are busily preparing more enzyme design puzzles, but this time with the intent of designing enzymes to aid in carbon fixation (aka taking CO2 out of the atmosphere).

We will try to contact g_s & aap to let them know about their accomplishments!

(I believe that everyone else is still active)

Thanks for the great suggestion!

What exactly did my teammates and I do in Puzzle 366 (Back Me Up 1)? I'm asking because pulling up my team's top-scoring evolver solution revealed that the helix contains too many aromatic side chains-- how is that not an artifact of the score function?

Pleased to see the work on CO2 fixation continuing: it would be really nice if the next generation have a world fit to live in.

For Puzzle 366 (Back Me Up 1), we put more significance on the kind of backbone structures produced by players than the specific amino acid sequences. The poly-aromatic residues were indeed an artifact of the score function, but it was working as expected on the backbone atoms. We took the player designed backbones and built libraries with varied side chains around them to test in lab, ultimately yielding increases in activity.

how it is done in real lab :D

We were able to fix the score function thanks to your discovery of these score function artifacts!

Hopefully you haven't come across any design puzzles since February 2011 (Puzzle 401: Quick Loop Puzzle) where you were able to create poly-Tryptophan helices that scored well.

Just to make sure:

In addition to the poly-tryptophan trick and the pi helix trick, has the EEEERRRR trick been investigated as well? As the name suggests, EEEERRRR refers to repeats of four consecutive glutamates followed by four consecutive arginines. Because this combination allows for easy formation of two side chain hydrogen bonds between residue n and residue n+4 (specifically, between the carboxyl O and two hydrogens on the guanidinium group), it scores very well on an exposed alpha helix and can be game-breaking at times in the past.

The EEEERRRR one has also been previously noted. Fixes are harder for this artifact because the n+4 salt bridge motif is natural and provides stability in helices, though EEEERRRR would not.

The link http://depts.washington.edu/bakerpg/drupal/node/424 appears to be broken. It returned a 'Page not found' message under the Baker laboratory banner.

I found the pdf file at http://depts.washington.edu/bakerpg/drupal/system/files/eiben12A.pdf