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Rosetta@home

BOINC project Rosetta@home: Main page News

Project News Jan 29, 2012 - Journal post from David BakerLast year we described in Science magazine the design of a new enzyme which catalyzes a chemical reaction called the Diels Alder reaction involving the formation of two carbon-carbon bonds. This reaction is interesting because no natural enzymes are known to catalyze the reaction. However, it wasn't a very good enzyme, and we asked FoldIt players to try to improve it. As described in Nature Biotechnology this month, remarkably FoldIt players were able to make the designed enzyme 20 times faster by inserting a completely new loop which helps the enzyme bind the chemicals it links together. The combination of Rosetta@Home and FoldIt is turning out to be powerful indeed for solving challenging problems in biomedicine!

Project News Jan 16, 2012 - Journal post from David BakerIn response to requests from many of you, we will be posting descriptions of the many scientific problems currently being tackled with Rosetta@Home on the Science message boards in the next couple of weeks--stay tuned! I also want to describe a new research direction we are now embarking on aimed at future cancer therapies. There are a small set of proteins which are frequently found at much higher levels than normal on the surface of cancer cells. We are starting to design small proteins which bind tightly to these tumor cell markers. If we are successful, we have collaborators who will be testing these proteins for their ability to target cancer cell killing agents to the tumors.

Project News Jan 13, 2012 - Rosetta@Home software updated to version 3.20. This should fix the graphical issues some users were seeing with version 3.19.

Project News Jan 02, 2012 - The hardware hosting the Rosetta@Home project is being moved from one datacenter to another on the UW campus. We are using this disruption to update the sagging, aging gear that runs the project. All of this will result in a few days of down time. We will work to keep the outage to a minimum, but you migh want to grab enough work for a 4-5 day period. We appreciate your patience, interest and continued contributions to our research. -KEL

Project News Dec 19, 2011 - Rosetta@Home software updated to version 3.19

Project News Oct 26, 2011 - David Baker receives UW Medicine's Inventor of the Year award. From the award announcement " the Inventor of the Year award is given to individuals who have translated research from the bench, through partnerships with the biomedical industry, to a product or process that has had a major impact on healthcare and the local economy" . Read more...

Project News Oct 26, 2011 - Rosetta@Home software updated to version 3.17

Project News Oct 22, 2011 - Journal post from David BakerToday's issue of Science magazine describes an exciting new approach to HIV vaccine design using Rosetta. In contrast with other viruses such as polio and influenza, inactivated HIV or HIV proteins have not worked as vaccines, and hence as you know there is currently no effective HIV vaccine. Our approach to vaccine design is to take the bits of the HIV surface protein that people make antibodies to, and using Rosetta graft them onto small stable scaffolds that can be made in large quantities and potentially could be useful as vaccines. We've shown earlier that this can be done straightforwardly with Rosetta if the bits of the HIV protein are contiguous along the sequence, but it is much harder if the antibody recognizes multiple bits close in three dimensions but far in sequence. In this paper we show how such "discontinuous" epitipes can be transferred from HIV gp120 to a simple scaffold protein. More work will be required to determine whether this or other vaccine candidates designed using this approach will be effective as HIV vaccines-let us all hope so!!

Project News Oct 6, 2011 - Journal post from David BakerA recent issue of Nature describes an exciting result from Rosetta@home in collaboration with the NMR spectroscopy laboratory of Lewis Kay in Toronto. Like almost all machines, proteins in order to carry out their functions have to move (change their conformation somewhat) but it has been extremely difficult to determine what these conformational changes are. Lewis Kay's group has developed new methods for getting experimental information on the higher energy very shortlived conformations proteins visit while carrying out their functions. This data is not sufficient to determine the structure of these "excited state" conformations using conventional methods. However, as the paper shows, we can use these experimental data to guide Rosetta and Rosetta@home structure calculations, and produce models of these states. We went one step further than this in the paper by using Rosetta design calculations to stabilize the excited state, and subsequent experiments confirmed the validity of the model. This combination of experimental NMR data, Rosetta structure calculations, and Rosetta design should be very powerful in understanding how proteins carry out their functions.