As you may have heard, the [Link] Institute for Protein Design was recently selected as part of [Link] 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 [Link] 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. Thank you, David Baker Director, Institute for Protein Design

By rosetta@home at 2019-07-16

Last week, a report was published in [Link] 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 [Link] 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 [Link] click here.

By rosetta@home at 2019-07-15

Last week, the [Link] Baker Lab in collaboration with the [Link] De Yoreo lab at PNNL published a report in [Link] 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 [Link] click here.

By rosetta@home at 2019-07-15