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.
Fluorescent proteins designed from scratch
Congrats to all Rosetta@home volunteers who contributed to a recent report in Nature describing the design of a completely artificial fluorescent beta-barrel protein. As described by one of the main authors, Anastassia, in this forum post:
The paper presents many “firsts” in computational protein design. It is the first de novo design of the beta-barrel fold (one of the most described folds in the past 35 years, yet mysterious until now). It is also the first de novo design of a protein tailored to bind a small-molecule, which requires very high accuracy in the placement of side chains on protein backbones assembled from scratch. Additionally, we could show that these new proteins could fold and function as expected in vivo! We hope that the advances described in the paper will further enable the de novo design of many biosensors and catalysts tailored for specific applications.
Thanks to all the Rosetta@home volunteers who contributed to the validation of our designed proteins and binding sites.
Here is the link to the IPD webpage that contains a copy of the paper. The work was also featured in the news articles below (the news in Science contains a video of one of our proteins glowing in living cells).
17 Sep 2018, 23:14:21 UTC · Discuss
Congrats to the collaborative WeFold group for their recent paper published in Nature Scientific Reports. Thank you to all R@h volunteers who contributed to this work.
Congrats to the WeFold group for their recent publication, An analysis and evaluation of the WeFold collaborative for protein structure prediction and its pipelines in CASP11 and CASP12, in Nature Scientific Reports. As CASP13 is currently in full swing, this article describes the results and analysis of the CASP11 and CASP12 WeFold coopetition (cooperation and competition) . Most of the models used by WeFold for CASP12 (and currently for CASP13) were generated by Rosetta@home volunteers. Congrats and Thank you!
3 Jul 2018, 0:13:42 UTC · Discuss
Rosetta Android version 4.10 released
This version uses a relatively recent version of the Rosetta source. It includes updates to the cyclic peptide folding protocol among other code updates and additions since the previous build. Please post comments and issues in this thread.
27 Apr 2018, 23:29:47 UTC · Discuss
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
©2018 University of Washington