Rosetta@home
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
About
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Statistics

    http://srv4.bakerlab.org/rosetta_cgi/cgi

User of the day                

Matthias Folster Profile
 
  Server Status as of 30 Jul 2016 1:22:22 UTC  
[ Scheduler running ]
Total queued jobs: 631,287
In progress: 1,152,378
Successes last 24h: 380,231
Users (last day ) :
1,066,255 (+2015)
Hosts (last day ) :
1,990,538 (+2080)
Credits last 24h :
53,637,081
Total credits :
46,437,758,404
TeraFLOPS estimate: 536.371

Jul 29, 2016
Predictor of the day: Congratulations to ce1197085 for predicting the lowest energy structure for workunit gr062216_EHEE_0574_fragments_fold_SAVE_ALL_OUT_388020_0 !

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News  

Jul 29, 2016
Another paper from the Baker lab in Science! Designed Protein Containers Push Bioengineering Boundaries.

"In this paper, former Baker lab graduate student Jacob Bale, Ph.D. and collaborators describe the computational design and experimental characterization of ten two-component protein complexes that self-assemble into nanocages with atomic-level accuracy. These nanocages are the largest designed proteins to date with molecular weights of 1.8-2.8 megadaltons and diameters comparable to small viral capsids. The structures have been confirmed by X-ray crystallography. The advantage of a multi-component protein complex is the ability to control assembly by mixing individually prepared subunits. The authors show that in vitro mixing of the designed subunits occurs rapidly and enables controlled packaging of negatively charged GFP by introducing positive charges on the interior surfaces of the two copmonents.

The ability to design, with atomic-level precision, these large protein nanostructures that can encapsulate biologically relevant cargo and that can be genetically modified with various functionalities opens up exciting new opportunities for targeted drug delivery and vaccine design." - from the IPD website.

More information can be found at this link.

Thank you all for your contributions!

Jun 17, 2016
A brand new paper from the Baker lab in Nature! Thank you yet again for your contributions, Rosetta@home volunteers. Although R@h was not directly used for these designs due to size and memory limitations, your contributions are instrumental in Rosetta development enabling such science. Thank you!

"Design of a hyperstable 60-subunit protein icosahedron" describes the design of a 20-sided nano-sized particle that could be used to deliver drugs or to develop powerful new vaccines.

Author and Baker lab graduate student Yang Hsia spoke on a Nature podcast on the work. Have a listen to hear about this awesome work from the protein design experts themselves! Links below.

Paper

Podcast Under 16 June 2016 "Protein football"

Accessible PDF of Nature paper


Jun 17, 2016
Journal post from David Baker

I recommend listening to graduate student Yang Hsia's podcast on designing protein footballs which you can find on the Nature web site this week to go along with his paper. (see Ratika's post for the link if you can't find it). Thank you all again for all of your contributions to our research-we couldn't do it without you!


May 10, 2016
We've come out with a breakthrough paper in Science titled 'De novo design of protein homo-oligomers with modular hydrogen-bond network-mediated specificity'.

This is an exciting and significant breakthrough for de novo protein design. A particular challenge for current protein design methods has been the accurate design of polar binding sites or polar binding interfaces, both of which require hydrogen bonding interactions. Hydrogen bond networks are governed by complex physics and energetic coupling, that until now, could not be computed within the scope of design. The computational method described in this paper, HBNet, now provides a general method to accurately design in hydrogen bond networks. This new capacity should be useful in the design of new enzymes, proteins that bind small molecules, and polar protein interfaces. Thanks Rosetta@home community for your participation and help!

The PDF of this article can be found here https://www.bakerlab.org/wp-content/uploads/2016/05/680.full_.pdf. An article on this work was also published in Geekwire http://www.geekwire.com/2016/uw-researchers-add-new-twists-protein-designs.

Apr 28, 2016
We'll be down for an hour or so for some maintenance. Sorry for any inconvenience.

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