Here! Well, not quite, which is why I'm looking for little green men, rather than folding.
I am a wet biochemist; one of the things I do is to get bacteria to make masses of a particular protein of interest, bash it all up into a goo, purify the protein of interest out of that then "re-fold" it to get it back into its proper shape, then crystalise it so we can use x-rays to get structures from, which then the computational folders can eventually use them to test out their models.
Here's one that I've been involved in, presented in as pretty a form as I know how to display it.
other things you can do is to try and design small molecules (drugs) that will interact with particular sites on that protein and test the strength of their binding in the computer, using programs like AutoDock, which I kind of have done, except I was using it to test interactions between two proteins. For this project, I managed to use 8 of my own Seti cores and another 12 cores at work for a solid two weeks of computing (would have been nice if I could submit this kind of thing to Folding at home eh?). Folding at home has done some of this kind of work, exampled in project 61 in their results page (
http://folding.stanford.edu/English/Papers).
As far as I know, the ability of folding algorithms to predict structures accurately is limited to probably 1/10th the size of the protein above, but its been a while since i read the papers; I see in Folding at home's results page that they folded residues (er think building blocks) 1-39 of NTL 9 (project 72), for comparison, the protein above is residues 32-466. So still a way to go yet, and the protein above isn't terribly large in the first place.
Hope this explains why I'd rather look for little green men and not extend my working hours more into my hobbies
Oh and for my own development, please give some feedback into how badly I communicated Science .....
