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.
Follow us on Twitter: @rosettaathome
Rosetta@home is not for profit.
Join Ralph@home to help improve this project.
Another publication in Nature describing the first de novo designed proteins with anti-cancer activity
A report was published in Nature last week describing the first de novo designed proteins with anti-cancer activity.
These compact molecules were designed to stimulate the same receptors as IL-2, a powerful immunotherapeutic drug, while avoiding unwanted off-target receptor interactions. We believe this is just the first of many computer-generated cancer drugs with enhanced specificity and potency.
R@h participants provided computing for forward folding experiments used in this study which helped validate designs. We'd like to congratulate and thank all R@h volunteers who contributed to this work! Thank you!
Read the full article here: https://www.nature.com/articles/s41586-018-0830-7 (PDF)
14 Jan 2019, 22:58:59 UTC · Discuss
Nature article on IPD work voted ‘2018 Reader’s Choice’
Readers of Nature’s News & Views selected an article about our work as their 2018 Reader’s Choice!
The article, written by Roberto Chica of University of Ottawa, does a fantastic job detailing our recent publication on de novo fluorescence-activating proteins — and the challenges of de novo protein design more generally.
4 Jan 2019, 1:06:51 UTC · Discuss
New publication in Nature: programmable heterodimers
A new report was recently published in Nature describing the design of proteins that mimic DNA.
Using computational design, heterodimeric proteins that form double helices with hydrogen-bond mediated specificity were created. When a pool of these new protein zippers gets melted and then allowed to refold, only the proper pairings form. They are all-against-all orthogonal. With these new tools in hand, it may be possible to construct large protein-based machines that self-assemble in predictable ways.
Read the full article here: https://www.nature.com/articles/s41586-018-0802-y (PDF)
We'd like to thank all Rosetta@home volunteers who contributed computing resources used in this work. Thank you!
4 Jan 2019, 0:57:58 UTC · Discuss
De novo design of self-assembling helical protein filaments
Another de novo design publication was released today describing the design of micron scale self-assembling helical filaments based on previously designed repeat proteins for which R@h participants contributed computing towards. Although R@h was not directly used for this study, R@h participants provided computing for related research. Thank you all for your continued contributions.
Read more here in Science.
9 Nov 2018, 19:40:30 UTC · Discuss
De novo design of jellyroll structures
Sorry for the late post. Last week the Baker lab and collaborators published the first example of proteins designed with non-local beta strand topology.
You can read more about this study here and the publication here.
Thanks to all Rosetta@home participants who contributed to this research.
8 Nov 2018, 23:02:02 UTC · Discuss
©2019 University of Washington