Results
Current Calculations What are we calculating right now? Check out our current calculations page or our projects summary page. |
Movies of simulation results We're working on a better site for the movies. At the moment, the only movies available and linked below. |
 |
Press coverage
|
Details about some of Folding@Home's success (more complete information can be found on our papers page):
| 2006 Folding in nanotubes . We have been studying the folding of proteins and peptides in confined spaces. We have several results in the "publishing pipeline" and the first one to get published is our results on peptides in nanotubes. We find a surprising result: confined water acts very differently than expected and acts to denature proteins! |  |
| 2004-2006 New methods for computational drug design. We have been developing new ways to calculate the free energy of protein-ligand binding (important to drug design) to unprecedented accuracy. Our first results published include the thesis of Michael Shirts and a recent paper with collaborators at Fujitsu. Several additional results will be following soon. |  |
| 2005 First results from Folding@Home cancer project published. We have been studying the p53 tumor surpressor and our first results on p53 have recently been published. You can find a summary and link to the paper on our papers page. To our knowledge, this is the first peer-reviewed results from a distributed computing project related to cancer. Thanks to the continued support of FAH donors, this is will be just the first of many cancer related works that will come from FAH. Roughly half of all known cancers result from mutations in p53. Our first work in the cancer area examines the tetramerization domain of p53. We predict how p53 folds and in doing so, we can predict which amino acid mutations would be relevant. When compared with experiments, our predictions have appeared to agree with experiment and give a new interpretation to existing data. |
Structure of the p53 dimer with the Leu330 mutant highlighted. Our simulations predict several mutations which would have a signifincat impact on the rate of folding of p53. This one, Leu330, has already been implicated in cancer. |
|
2000-2006 Accurate prediction of folding rates for many small proteins To summarize our results, one can just look at our rate predictions for the folding of small proteins. More information (and a review paper) will be placed on our papers page when available. |
 |
|
2002 Folding simulations of the villin headpiece We have successfully folded a small 36-residue alpha helical protein: the villin headpiece. We will soon post our paper (once the referee process has been completed). For now, check out our special page on our villin folding simulation results. |
 |
|
2002 Folding simulations of small beta hairpins, including the C-terminal beta hairpin of protein G and Trp Zippers Our beta hairpin work was the first results from folding@home to be published. You can get the paper from our papers page. |
 |
|
2002 Folding of a small beta-beta-alpha fold We have successfully folded a small protein with a beta-beta-alpha fold. We will soon post our paper (once the referee process has been completed). For now, you can check out some of our movies. |
 |
|
2000 UNFOLDING OF THE DNA BINDING DOMAIN OF HIV INTEGRASE HIV uses proteins to insert its genetic code into our DNA. The DNA binding domain of HIV integrase (below) is the protein which HIV uses to grab onto our DNA such that it can then connect its genetic code into ours. This movie shows a single trajectory of the unfolding of this protein under extreme denaturing conditions.
|
|
|
2000 FOLDING OF AN ALPHA HELIX USING DISTRIBUTED DYNAMICS Since our distributed dynamics method is extremely computationally intensive, we have first demonstrated its potential by folding the smallest protein one could imagine --- a single alpha helix. We have two simulation results presented here (20-mers and 30-mers). 20-mer of poly-alanine: MPEG -- 30-mer of poly-alanine: MPEG
|
 |
|
2000-2005 FOLDING OF A NONBIOLOGICAL POLYMER This polymer was designed to fold into a helix, much like the protein above. Here we show a simulation of two of them folding and then assembling into a tube, and then separating.
|
 |
|
2000 UNFOLDING OF DESIGNED PROTEIN This protein was designed by the Mayo Lab to fold into a "zinc finger" fold (a protein fold which typically binds to DNA).
|
 |
