What is Rosetta@home?
Play the FoldIt interactive game!

Rosetta@home needs your help to determine the 3-dimensional shapes of proteins in research that may ultimately lead to finding cures for some major human diseases. By running the Rosetta program on your computer while you don't need it you will help us speed up and extend our research in ways we couldn't possibly attempt without your help. You will also be helping our efforts at designing new proteins to fight diseases such as HIV, Malaria, Cancer, and Alzheimer's (See our Disease Related Research for more information). Please join us in our efforts! Rosetta@home is not for profit.
Follow us on Twitter: @rosettaathome        

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Join Rosetta@home
  1. Rules and policies
  2. System requirements
  3. Download, install, and run BOINC
    When prompted, select Rosetta@home from the list of projects.
  4. A welcome from David Baker
  5. Donate
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User of the day                

VioletsAreBlue Profile
South Korean residing in somewhere in Europe as of February 2017.
Intrested in biology, chemistry, and quantum physics.
  Server Status as of 28 Feb 2017 16:00:06 UTC  
[ Scheduler running ]
Total queued jobs: 8,252,147
In progress: 327,046
Successes last 24h: 143,213
Users (last day ) :
1,239,848 (+101)
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Feb 28, 2017
Predictor of the day: Congratulations to Nomad for predicting the lowest energy structure for workunit CXCX_O-C2-C4_scad4_tj10C4G1_1_monomer_0010_1chain.ff1_abinitio_SAVE_ALL_OUT_466407_0 !

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Feb 27, 2017
Journal post from David Baker

NOVA recently featured some of the work that all of you are contributing to: (the 8 minute segment on our work starts at 20:30)

The Economist also had an article on the work you are contributing to:

Your contributions are highlighted particularly clearly in the Geekwire article:
which is titled "Big data (and volunteers) help scientists solve hundreds of protein puzzles"

Jan 20, 2017
Journal post from David Baker

Hi Everybody!

this has been a good week with papers in this and last weeks Science magazine. your contributions were essential for both breakthroughs! here is some of the press you might find interesting:

thank you again for your invaluable contributions to this research!!


Jan 19, 2017
More good news!

Our paper titled "Protein structure determination using metagenome sequence data" was released today in the journal Science. We would like to thank all Rosetta@Home participants who provided the computing required for this work. In the paper, we describe using predicted co-evolving contacts from metagenomics sequence data and Rosetta to accurately predict the structures for 622 protein families that are not represented in the PDB. Among these structures, over 100 were new folds. Since experimental protein structure determination is costly and often difficult, this study highlights the ability to use computational methods with metagenomics data for reliably structure determination. With the rapidly growing size of genomics data, the future in mapping the structure space of protein families looks bright! Thank you Rosetta@Home participants!

Here is an interesting perspective written by Johannes Söding about the paper and it's significance, "Big-data approaches to protein structure prediction".

and related news articles:

  • Big data (and volunteers) help scientists solve hundreds of protein puzzles
  • Seeking Structure With Metagenome Sequences
  • Decoding the Origami That Drives All Life

    Jan 9, 2017
    Happy New Year!

    As many of you are likely aware of, we had an outage yesterday that we are just recently recovering from. The University of Washington campus and surrounding Seattle area had a power outage that lasted for a couple hours. For more info about the outage click here. It may take a day or so to get back to normal operation. Sorry for any inconvenience.

    Sep 23, 2016
    Some good news!

    We recently published an article in Nature titled "Accurate de novo design of hyperstable constrained peptides". We would like to thank all Rosetta@Home participants for their help with this work. In the paper, we present computational methods for designing small stapled peptides with exceptional stabilities. These methods and designed peptides provide a platform for rational design of new peptide-based therapeutics. Constrained (stapled) peptides combine the stability of conventional small-molecule drugs with the selectivity and potency of antibody therapeutics. The ability to precisely design these peptides in custom shapes and sizes opens up possibilities for "on-demand" design of peptide-based therapeutics.

    Other developments described in the paper:

  • We can now accurately design 18-47 amino acid peptides that incorporate multiple cross-links.
  • We can now design peptides that incorporate unnatural amino acids. Specifically, we designed peptides with a mix of natural L-amino amino acids and D-amino acids (mirror images of L-amino acids). D-amino acids tend to provide better protease resistance and lower immunogenicity; both of which are desired properties in a therapeutic peptide. Unnatural amino acids also let us sample much more diverse shapes and functions.
  • We can now design peptides that are cyclized via a peptide bond between their N- and C-terminus. Cyclic peptides provide increased resistance against exopeptidases as they have no free ends, and thus are ideal candidates for engineering peptide therapeutics.

    We are now working to use these computational methods for designing peptides that target therapeutically relevant targets, such as, enzymes that impart antibiotic resistance in pathogenic bacteria.

    Structure prediction runs on Rosetta@Home for these designed peptide models played a key role in selection of good designs that were experimentally synthesized and characterized. Thank you all for your help in making this work possible! -- Gaurav B.

    For more information:

  • IPD News.
  • Nature paper "Accurate de novo design of hyperstable constrained peptides".
  • Nature review "The coming of age of de novo protein design".


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