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.
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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Rosetta@home is not for profit.
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Designing shape-shifting proteins
Thank you to all R@h participants who provided much of the computing used in a recent study published in PNAS describing the design of proteins that adopt more than one well-folded structure, reminiscent of viral fusion proteins.
For more infomation, click here.
19 Mar 2020, 0:47:01 UTC · Discuss
Rosetta's role in fighting coronavirus
Thank you to all R@h volunteers for your contributions to help accurately model important coronavirus proteins. The collective computing power that you provide through R@h helps academic research groups world wide model important protein structures like these.
From a recent IPD news post:
"We are happy to report that the Rosetta molecular modeling suite was recently used to accurately predict the atomic-scale structure of an important coronavirus protein weeks before it could be measured in the lab. Knowledge gained from studying this viral protein is now being used to guide the design of novel vaccines and antiviral drugs."
Since the release of SARS-CoV-2 genome sequences in late January, a number of important corona virus proteins like the one described above have been modeled on R@h volunteer computers. A list of these proteins is provided by the Seattle Structural Genomics Center for Infectious Disease (SSGCID).
24 Feb 2020, 18:19:59 UTC · Discuss
The Audacious Project
As you may have heard, the Institute for Protein Design was recently selected as part of The Audacious Project. This large-scale philanthropic collaboration, which is the successor to the TED Prize, surfaces and funds projects with the potential to change the world.
As a result, we are expanding our Seattle-based team of scientists and engineers who will work together to advance Rosetta, our software for protein design and structure prediction. The funding will also allow us to invest in the equipment, supplies and lab space needed to design and test millions of synthetic proteins.
What challenges will we be tackling? Watch my TED talk to find out.
All of this work — like everything we do — will depend on you, the participants in Rosetta@home. Whether it’s creating custom nanomaterials or safer cancer therapies, we rely on the Rosetta@home distributed computing platform. We cannot thank you enough for taking the time to be a part of this exciting research, and we hope you tell at least one friend that they too can play a role in the protein design revolution just by running Rosetta@home.
Director, Institute for Protein Design
16 Jul 2019, 22:18:18 UTC · Discuss
Coevolution at the proteome scale
Last week, a report was published in Science describing the identification of hundreds of previously uncharacterized protein–protein interactions in E. coli and the pathogenic bacterium M. tuberculosis. These include both previously unknown protein complexes and previously uncharacterized components of known complexes. This research was led by postdoctoral fellow Qian Cong and included former Baker lab graduate student Sergey Ovchinnikov, now a John Harvard Distinguished Science Fellow at Harvard. Rosetta@home was used for much of the computing required for this work. Congratulations and thank you to all R@h volunteers.
For more information about this work click here.
15 Jul 2019, 19:23:58 UTC · Discuss
Protein arrays on mineral surfaces
Last week, the Baker Lab in collaboration with the De Yoreo lab at PNNL published a report in Nature describing the design of synthetic protein arrays that assemble on the surface of mica, a common and exceptionally smooth crystalline mineral. This work provides a foundation for understanding how protein-crystal interactions can be systematically programmed. Although R@h was not directly used for this research, previously designed subunits were validated using R@h. Congratulations to all R@h volunteers and thank you for your continued contributions.
For more details click here.
15 Jul 2019, 19:12:28 UTC · Discuss
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