You don’t have to be a scientist to do science.

By simply running a free program, you can help advance research in medicine, clean energy, and materials science.

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How does it work?

By running Rosetta@home on your computer when you're not using it you will speed up and extend our efforts to design new proteins and to predict their 3-dimensional shapes. Proteins are the molecular machines and building blocks of life. You can read more about protein folding and design here.

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User of the Day

User profile Profile SlumLord
The above picture is of my dog Petra (R.I.P.) and I. I am a 41 year old webMethods software developer who works in Battle Creek, Michigan. The small...

Predictor of the day

Predictor of the day: Congratulations to jim crum for predicting the lowest energy structure for workunit bhoh_a_1_cd98_....
23 Apr 2018, 0:00:00 UTC · Discuss

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As of 23 Apr 2018, 19:01:39 UTC [ Scheduler running ]
Total queued jobs: 13,560,302
In progress: 521,738
Successes last 24h: 229,684
Users (last day ): 1,277,038 (+73)
Hosts (last day ): 2,298,020 (+338)
Credits last 24h : 40,709,986
Total credits : 66,035,857,820
TeraFLOPS estimate: 407.100


Science opinion article about protein engineering and David Baker

Checkout a recent Bloomberg science opinion article about some of the science behind this project, protein engineering, and David Baker, titled Protein Engineering May Be the Future of Science.

28 Mar 2018, 17:51:52 UTC · Discuss

Rosetta 4.07 released

This version contains a bug fix for the cyclic peptide folding protocol. Please post any issues/bugs regarding this application in this thread.
27 Feb 2018, 18:33:12 UTC · Discuss

Charity Event 2018

The Charity Team has chosen Rosetta@home for their 10th annual event to receive extended computation support for 2 weeks (January 14th 2018, 0.01h to January 27th 2018, 23.59h UTC). To participate, BOINC members are asked to leave their ‘Home Teams‘ and join the Charity Team to crunch Rosetta@home together without the normal ‘Race Conditions‘ during this time frame.

To join the Charity Team at Rosetta@home please click here:

You can find more information on the Charity Event forums:
and about the Charity Team:

Stats are also available at:
Team Stats (BoincStats):
User Stats (Sébastien):
Comparison Stats (XSmeagolX):

Many thanks to the Charity Team for choosing Rosetta@home for their annual event!

4 Jan 2018, 0:30:08 UTC · Discuss

The New York Times recently published an article about David Baker and Rosetta

Scientists Are Designing Artisanal Proteins for Your Body

The human body makes tens of thousands of cellular proteins, each for a particular task. Now researchers have learned to create custom versions not found in nature....

2 Jan 2018, 19:31:43 UTC · Discuss

Recent Science and Nature publications. Congrats!

Two research publications were released last week in Science and Nature. The Science publication describes work which relied on computations from Rosetta@home most of which were from Android devices. The Nature publication did not directly use Rosetta@home due to the large size of the designs but used Rosetta. Congrats and thank you for your contributions!

Comprehensive computational design of ordered peptide macrocycles. As described in the abstract, macrocyclic peptides composed of l- and d-amino acids were designed by near-exhaustive backbone sampling followed by sequence design and energy landscape calculations. More than 200 designs were predicted to fold into single stable structures, many times more than the number of currently available unbound peptide macrocycle structures. Nuclear magnetic resonance structures of 9 of 12 designed 7- to 10-residue macrocycles, and three 11- to 14-residue bicyclic designs, are close to the computational models. The results provide a nearly complete coverage of the rich space of structures possible for short peptide macrocycles and vastly increase the available starting scaffolds for both rational drug design and library selection methods.

Read more from UW Medicine News.

Evolution of a designed protein assembly encapsulating its own RNA genome. As described in the abstract, synthetic nucleocapsids composed of icosahedral protein assemblies with positively charged inner surfaces were computationally designed. The ability of these nucleocapsids to evolve virus-like properties by generating diversified populations and selecting for improved genome packaging and fitness against nuclease challenge was also explored. The results show that there are simple evolutionary paths through which protein assemblies can acquire virus-like genome packaging and protection. Considerable effort has been directed at ‘top-down’ modification of viruses to be safe and effective for drug delivery and vaccine applications; the ability to design synthetic nanomaterials computationally and to optimize them through evolution now enables a complementary ‘bottom-up’ approach with considerable advantages in programmability and control.

18 Dec 2017, 19:20:52 UTC · Discuss

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