Renamed section. Removed verbatim copy-paste from R@H website (most of which reiterates stuff from 'Project significance') to make way for more specific discussion of disease-related research |
→Disease-related research: Adding subsections for malaria and anthrax |
||
Line 34: | Line 34: | ||
A component of the Rosetta software suite, RosettaDock,<ref>{{cite journal | title=Improved side-chain modeling for protein–protein docking | author=Wang et al | journal=Protein Science | year=2005 | volume=14 | issue=5 | pages=1328-1339 | url=http://www.proteinscience.org/cgi/content/full/14/5/1328 | doi=10.1110/ps.041222905}}</ref><ref>{{cite journal | title=Protein–Protein Docking with Simultaneous Optimization of Rigid-body Displacement and Side-chain Conformations | author=Gray et al | journal=Journal of Molecular Biology | year=2003 | volume=331 | issue=1 | pages=281-299 | url=http://dx.doi.org/10.1016/S0022-2836(03)00670-3 | doi=10.1016/S0022-2836(03)00670-3}}</ref><ref>{{cite journal| title=Progress in protein-protein docking: Atomic resolution predictions in the CAPRI experiment using RosettaDock with an improved treatment of side-chain flexibility | author=Schueler-Furman et al | journal=Proteins | year=2005 | volume=60 | issue=2 | pages=187-194 | url=http://www3.interscience.wiley.com/cgi-bin/fulltext/110548114/HTMLSTART | doi=10.1002/prot.20556}}</ref> was used to model docking between an [[antibody]] ([[immunoglobulin G]]) and a surface protein expressed by [[herpes simplex virus 1]] (HSV-1) which serves to degrade the antiviral antibody. The protein complex predicted by RosettaDock closely agreed with hard-gotten experimental models, leading researchers to conclude that the docking method has potential in addressing some of the problems that X-ray crystallography has with modeling protein-protein interfaces.<ref>{{cite journal | title=Crystal Structure of the HSV-1 Fc Receptor Bound to Fc Reveals a Mechanism for Antibody Bipolar Bridging | author=Sprague et al | journal=PLoS Biology | volume=4 | issue=6 | pages=e148 | url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1450327 | doi=10.1371/journal.pbio.0040148}}</ref> |
A component of the Rosetta software suite, RosettaDock,<ref>{{cite journal | title=Improved side-chain modeling for protein–protein docking | author=Wang et al | journal=Protein Science | year=2005 | volume=14 | issue=5 | pages=1328-1339 | url=http://www.proteinscience.org/cgi/content/full/14/5/1328 | doi=10.1110/ps.041222905}}</ref><ref>{{cite journal | title=Protein–Protein Docking with Simultaneous Optimization of Rigid-body Displacement and Side-chain Conformations | author=Gray et al | journal=Journal of Molecular Biology | year=2003 | volume=331 | issue=1 | pages=281-299 | url=http://dx.doi.org/10.1016/S0022-2836(03)00670-3 | doi=10.1016/S0022-2836(03)00670-3}}</ref><ref>{{cite journal| title=Progress in protein-protein docking: Atomic resolution predictions in the CAPRI experiment using RosettaDock with an improved treatment of side-chain flexibility | author=Schueler-Furman et al | journal=Proteins | year=2005 | volume=60 | issue=2 | pages=187-194 | url=http://www3.interscience.wiley.com/cgi-bin/fulltext/110548114/HTMLSTART | doi=10.1002/prot.20556}}</ref> was used to model docking between an [[antibody]] ([[immunoglobulin G]]) and a surface protein expressed by [[herpes simplex virus 1]] (HSV-1) which serves to degrade the antiviral antibody. The protein complex predicted by RosettaDock closely agreed with hard-gotten experimental models, leading researchers to conclude that the docking method has potential in addressing some of the problems that X-ray crystallography has with modeling protein-protein interfaces.<ref>{{cite journal | title=Crystal Structure of the HSV-1 Fc Receptor Bound to Fc Reveals a Mechanism for Antibody Bipolar Bridging | author=Sprague et al | journal=PLoS Biology | volume=4 | issue=6 | pages=e148 | url=http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1450327 | doi=10.1371/journal.pbio.0040148}}</ref> |
||
⚫ | |||
⚫ | |||
In research involved with the [[Grand Challenges in Global Health]] initiative,<ref>{{cite web | title=Homing Endonuclease Genes: New Tools for Mosquito Population Engineering and Control | url=http://www.gcgh.org/ControlInsect/Challenges/GeneticStrategy/Pages/EndonucleaseGenes.aspx}}</ref> Rosetta has also been used to computationally design novel [[Intragenomic_conflict#Homing_endonuclease_genes | homing endonuclease]] proteins, which could eradicate ''[[Anopheles gambiae]]'' or otherwise render the mosquito unable to transmit [[malaria]].<ref>{{cite journal | title=Homing endonuclease mediated gene targeting in Anopheles gambiae cells and embryos | author=Windbichler et al | journal=Nucleic Acids Research | year=2007 | volume=35 | issue=17 | pages=5922-5933 | url=http://nar.oxfordjournals.org/cgi/content/full/35/17/5922?ck=nck | doi=10.1093/nar/gkm632 }}</ref> Being able to model and alter protein-DNA interactions, like those of homing endonucleases, gives computational protein design methods like Rosetta an important role in [[gene therapy]].<ref>{{cite journal | journal=Computational redesign of endonuclease DNA binding and cleavage specificity | author=Ashworth et al | title=Computational redesign of endonuclease DNA binding and cleavage specificity | journal=Nature | year=2006 | volume=441 | url=http://www.nature.com/nature/journal/v441/n7093/full/nature04818.html | doi=10.1038/nature04818}}</ref> |
|||
⚫ | |||
===Anthrax=== |
|||
RosettaDock was used in conjunction with experimental methods to model interactions between three proteins -- lethal factor (LF), edema factor (EF) and protective antigen (PA) -- that make up [[anthrax toxin]]. The computational model accurately predicted docking between LF and PA, helping to establish which [[protein domain | domains]] of the respective proteins are involved the LF-PA complex. This insight was eventually used in research resulting in improved anthrax vaccines.<ref>{{cite journal | title=A model of anthrax toxin lethal factor bound to protective antigen | author=Lacy et al | journal=Proc. Natl. Acad. Sci. USA | year=2005 | volume=102 | issue=45 | pages=16409-16414 | url=http://www.pnas.org/content/102/45/16409.full | doi=10.1073/pnas.0508259102}}</ref><ref>{{cite journal | title=Human Monoclonal Antibodies against Anthrax Lethal Factor and Protective Antigen Act Independently To Protect against Bacillus anthracis Infection and Enhance Endogenous Immunity to Anthrax | author=Albrecht et al | journal=Infection and Immunity | year=2007 | volume=75 | issue=11 | pages=5425-5433 | url=http://iai.asm.org/cgi/content/full/75/11/5425 | doi=10.1128/IAI.00261-07}}</ref> |
|||
⚫ | |||
===Amyloid-related illnesses=== |
|||
<ref>{{cite journal | title=The 3D profile method for identifying fibril-forming segments of proteins | author=Thompson et al | journal=Proc. Natl. Acad. Sci. USA | year=2006 | volume=103 | issue=11 | pages=4074-4078 | url=http://www.pnas.org/content/103/11/4074.full | doi=10.1073/pnas.0511295103}}</ref> |
|||
Another component of Rosetta, RosettaDesign, |
|||
== |
|||
<ref>{{cite journal | title=The RosettaDock server for local protein–protein docking | author=Lyskov S, Gray JJ | journal=Nucleic Acids Research | volume=36 | issue=Web Server issue | pages=W233-W238 | url=http://nar.oxfordjournals.org/cgi/content/full/36/suppl_2/W233 | doi=10.1093/nar/gkn216}}</ref> |
<ref>{{cite journal | title=The RosettaDock server for local protein–protein docking | author=Lyskov S, Gray JJ | journal=Nucleic Acids Research | volume=36 | issue=Web Server issue | pages=W233-W238 | url=http://nar.oxfordjournals.org/cgi/content/full/36/suppl_2/W233 | doi=10.1093/nar/gkn216}}</ref> |
||
--> |
--> |
Revision as of 04:39, 8 July 2008
Rosetta@home is a distributed computing project on the BOINC platform, run by the Baker laboratory at the University of Washington. With the help of over 90,000 volunteer computers processing over 66 TFLOPS on average as of July 1, 2008,[1] Rosetta@home aims to computationally predict protein structures and design new proteins to fight a range of diseases.[2]
Baker Lab
Baker Laboratory (website) is based at the University of Washington.
The principal investigator is David Baker, Professor of Biochemistry at the University of Washington and Howard Hughes Medical Institute investigator, who was elected to the United States National Academy of Sciences in April 2006.
The BakerLab scientific team [1] includes post-docs Phil Bradley, Jim Havranek, Bill Schief, Vanita Sood, Bin Qian, Eric Althoff, Daniela Roethlisberger, John Karanicolas, as well as numerous graduate students and visiting scientists.
Computing platform
Both the Rosetta@home application and the Berkeley Open Infrastructure for Network Computing (BOINC) distributed computing platform are available for the Microsoft Windows, Linux and Macintosh platforms (BOINC also runs on several other platforms, e.g. FreeBSD[3]). Participation in Rosetta@home requires at least a 500 MHz or higher CPU, 200 MB of free disk space, 256 MB of RAM, and Internet connectivity.[4] As of July 1, 2008, the current version of the Rosetta application is 5.98[5] and the current BOINC program version is 5.10.[3]
Project significance
With the completion of the Human Genome Project, scientists have only a 'flat' view of the primary structure (amino acid sequence) of proteins that make up the working parts of all human cells. In order to better understand a protein's function aid in rational drug design, scientists need to know the protein's 3-dimensional, tertiary structure.
Protein 3D structures are currently determined experimentally through X-ray crystallography or nuclear magnetic resonance (NMR). The process is slow (it can take weeks or even months to figure out how to crystallize a protein for the first time) and comes at high cost ($20,000-$100,000 USD per protein[citation needed]). Unfortunately, the rate at which new sequences are discovered far exceeds the rate of structure determination -- out of more than 6,600,000 protein sequences available in the NCBI Non-Redundant Protein database, less than 48,000 proteins' 3D structures have been solved and deposited in the Protein Data Bank, the main repository for structural information on proteins.[6] One of the main goals of Rosetta@home is to predict protein structures with the same accuracy as existing methods, but in a way that requires significantly less time and money.
Head scientist Prof. David Baker wrote in his Rosetta@home journal on Mar 3, 2006:
- "The protein structure prediction problem is perhaps the longest standing problem in molecular biology. It has been known for forty years that the structures of proteins are determined by their amino acid sequences, but as recently as five or six years ago it was generally thought that the prediction problem was completely intractable as very little progress had been made. Starting about this time we showed in the CASP blind tests that with the Rosetta low resolution structure prediction method rough models could be built for small proteins that in some cases were reasonably similar in topology to the true structure, but the predicted structures were never accurate at the atomic level. We have worked for the past five years on developing high resolution refinement methods that could take these rough models and refine them to much higher accuracy. This goal remained elusive for the first few years, but about a year and a half ago we made a breakthrough and found that we could make very accurate predictions for some proteins using a trick that involves folding not only the sequence of the protein of interest but also the sequences of a large number of evolutionarily related homologs. Using this method we made the first high accuracy ab initio structure prediction in CASP (the last target in CASP6) and did further tests which showed accurate predictions for 6 of 16 proteins which were published in Science last year.[7]
- However, this work did not achieve the goal of predicting structure accurately from the amino acid sequence of a protein alone as we had to resort to evolutionary information. Achieving this goal has been the central aim of Rosetta@home thus far, and as I said above it is almost a "holy grail" of computational biology. So now, for quite a few proteins we are coming close to predicting structure from their amino acid sequences without any other information is pretty breathtaking."
By participating in the Rosetta@home project, volunteers help verify and develop these new protein structure prediction algorithms.
Herpes simplex virus 1
A component of the Rosetta software suite, RosettaDock,[8][9][10] was used to model docking between an antibody (immunoglobulin G) and a surface protein expressed by herpes simplex virus 1 (HSV-1) which serves to degrade the antiviral antibody. The protein complex predicted by RosettaDock closely agreed with hard-gotten experimental models, leading researchers to conclude that the docking method has potential in addressing some of the problems that X-ray crystallography has with modeling protein-protein interfaces.[11]
Malaria
In research involved with the Grand Challenges in Global Health initiative,[12] Rosetta has also been used to computationally design novel homing endonuclease proteins, which could eradicate Anopheles gambiae or otherwise render the mosquito unable to transmit malaria.[13] Being able to model and alter protein-DNA interactions, like those of homing endonucleases, gives computational protein design methods like Rosetta an important role in gene therapy.[14]
Anthrax
RosettaDock was used in conjunction with experimental methods to model interactions between three proteins -- lethal factor (LF), edema factor (EF) and protective antigen (PA) -- that make up anthrax toxin. The computational model accurately predicted docking between LF and PA, helping to establish which domains of the respective proteins are involved the LF-PA complex. This insight was eventually used in research resulting in improved anthrax vaccines.[15][16]
About the ROSETTA Software Suite
Description
- Rosetta is a combination of two software elements. Rosetta ab initio predicts the three-dimensional structure of a folded protein from its linear sequence of amino acids. Numerous software tools around the ab initio concept have also been created that facilitate protein structure prediction. Rosetta combines the Rosetta ab initio structure prediction method with Nuclear Magnetic Resonance (NMR) experimental data for rapid backbone structure determination. Rosetta Design is a useful tool in creating better proteins by determining amino acid sequences that are good for a particular protein structure. It can also be used to enhance protein stability and create alternative sequences for naturally occurring proteins.
- The Rosetta codes are available to academics free of charge under a non-exclusive license while industry may obtain Rosetta through a non-exclusive license.
Development Background
- Under the aegis of David Baker, who is a Howard Hughes Medical Institute investigator as well as a professor in the Department of Biochemistry, numerous faculty, postdocs, graduate students, and undergraduates have worked on the Rosetta project over the past nine years. The result has been an highly collaborative research program hosted at the Baker Laboratory and enriched by its many contributors.
- Funding for the development of Rosetta was provided by the Packard Foundation, the National Science Foundation, and the National Institutes of Health.
Collaborative projects
The Human Proteome Folding Project (HPF) is a collaborative effort between New York University (Bonneau Lab), the Institute for Systems Biology (ISB) and the University of Washington (Baker Lab). HPF is running on IBM's World Community Grid (WCG) and on United Devices' grid.org.
HPF Phase-1 applied Rosetta v4.2x software on the human genome and 89 other genomes. It started in November 2004 and ended in July 2006. HPF Phase-2 (HPF2) will apply the latest Rosetta v5.x software in higher resolution, "full atom refinement" mode, concentrating on cancer biomarkers (proteins found at dramatically increased levels in cancer tissues), human secreted proteins and malaria.
- "The Baker laboratory at the University of Washington has developed a protein folding program named Rosetta. It has 3 major sections. The first section tries to fold a protein, going from a long string of amino acids to a crumpled up 3D structure. The second section tries to reverse this process. Given the surface of a crumpled up protein molecule, it attempts to design a chain of amino acids that will fold up to form that molecule. The third section tries to dock 2 different protein molecules to see how they will interact with each other.
- A number of universities (such as the University of Warsaw) and research institutes use this Rosetta program for different purposes (see Rosetta Commons at http://www.rosettacommons.org/ ). David Baker maintains a server on the Internet called the Robetta server ([2]) which allows other scientists to use Rosetta for their projects without maintaining local servers with Rosetta.
- Recently (3Q05) the Baker Lab has started a BOINC project named Rosetta@home ( http://boinc.bakerlab.org/rosetta/ ). The Baker Lab only has a 500-node Linux cluster, so it is very time-consuming to test variations while trying to improve Rosetta. The first section of Rosetta which folds proteins (called the ab initio prediction section) uses 2 methods. The first method is a speedy low resolution method. The second method is a computationally intensive high resolution method which takes a fold prediction from the low resolution method and attempts to refine it to produce a more accurate prediction. The cluster of computers created for Rosetta@home is used to test various improvements in the high resolution method. Eventually, Dr. Baker also intends to use this cluster to run queries from other scientists that are currently queued up to run on the Rosetta server.
- Rosetta has been producing the most accurate computer predictions of protein folds, as you can see at CASP6. The most accurate predictions are still made by human scientists, assisted by computer programs, but like human chess players, the computers are putting some pressure on them. Also see the 'Gene Machine' in the July 2001 issue of Wired
- Now, getting down to particulars. Where do we come in? The Institute for Systems Biology (ISB) in Seattle, WA, USA, has started a project called the Human Proteome Folding Project (HPF) to fold all the unknown proteins found in the human genome plus a number of proteins from 80 other genomes. See HPF
- This project uses the low resolution method of protein folding that is in the ab initio section of Rosetta. Each unknown protein is folded to produce about 10,000 predictions. Variable conditions are established by a random seed. Both grid.org and the World Community Grid are running this project for ISB. Each Work Unit makes 100-500 fold predictions for a previously unknown protein. The ISB creates a batch of proteins and puts it on the ISB server. Then either grid.org or WCG downloads the batch, sends out the work units, reassembles the results returned and finally uploads the corresponding batch of results back to the ISB server.
- Both grids (WCG and grid.org) are using the same version of Rosetta to fold the proteins. There were some bug fixes made in Rosetta back in December 2004. The WCG took the lead and then sent the patched version to grid.org which beta tested the new version, then deployed it in January 2005. This was the only cross-grid transfer of Rosetta code that I know of since the HPF project went live.
- There is a future project being readied to run on the World Community Grid that will use the new high resolution folding method being developed at Rosetta@home to refine the folding predictions made by HPF for some selected proteins. It is currently (and unimaginatively) being referred to as HPF2." source
Differences between protein research projects
Protein structure prediction projects such as Rosetta@home aim to specify what the final tertiary structure will be, from their amino acid sequences. Only then can biomed scientists deduce each protein's role / functionality in cell processes.
Rosetta@Home and Predictor@home are similar in that they both seek to predict the 3D structure. Rosetta uses energy functions to find the lowest or most stable state and Predictor uses Monte Carlo simulations using a knowledge-based force field, based upon a simplified lattice model.
Currently Rosetta is among the most accurate protein prediction methods, as evidenced in recent biennial CASP experiments (see chart comparing Rosetta and Predictor accuracy).
Folding@home is an advanced Computational Chemistry project using molecular dynamics (the laws of physics) to study the dynamics of protein folding and understand misfolding (aggregation) diseases such as Alzheimer's. Quote from Dr. Vijay S. Pande in the Folding@home forums:
- I know Baker and Ranganathan and their work very well and (like the rest of the protein community) find their work very important and impressive. However, Rosetta@home and Folding@Home are addressing very different problems.
- Rosetta only predicts the final folded state, not how do proteins fold (and Rosetta has nothing to do with protein misfolding). Thus, those methods are not useful for the questions we're interested in and the diseases we're tackling (Alzheimer's Disease and other aggregation related diseases).
- Also, one should note that accurate computational protein structure prediction is still very challenging compared to what one can do experimentally, whereas the information obtained from Folding@home on the nature of folding and misfolding pathways matches experiment (e.g. with quantitative validation in rates, free energy, etc) and then goes beyond what experiment can tell us in that arena. While Rosetta has gone a long way and is a very impressive project, given the choice between a Rosetta predicted structure and a crystal structure, one would always choose the crystal structure. I bet that will be changing due to their great efforts, but that may still be a ways off for that dream to be realized.
- So, both are valuable projects IMHO, but addressing very different questions. I think there are some misunderstandings out there, though. Some people think FAH is all about structure prediction (which it is not -- that's Rosetta's strength) and some think Rosetta is about misfolding related disease (which it's not, that's Folding@Home's strength). Hopefully this post helps straighten some of that out.
Features and Issues
Features related to the current version
- Since March 2006 the project uses variable run time work units, using the same raw protein data, with each unit being approximately 3 MB. Each work unit now runs for a defined period of CPU time (with the default CPU run time being 3 hours) calculating as many predicted protein structures - termed "models" - as the computer can create during this time period. A slow PC might compute only one model, whereas a fast PC over 100 models.
- Each work unit can run for between three and 24 hours, with the exact runtime being user-configurable.
- This CPU time option was added to allow participants on dialup Internet or operating large networks of PCs or "crunching farms" to drastically reduce Internet traffic from 1 GB per month per Pentium 4 (running 24/7) to 1/10th of that and even less.
- Users also have the option to change the frame rate and CPU use for graphics. The default frame rate is 10 frame/s.
- A new graphics version is available for Mac OS X users.
- Rosetta will consume between 40 MB and 140 MB of memory. The biggest units, which are very rare, need up to 250 MB of memory.
See also
- Protein structure prediction
- Protein folding
- CASP
- Drug design
- Human Proteome Folding Project
- Predictor@home
- Folding@home
- SIMAP
- Grid computing
- List of distributed computing projects
- BOINC
References
- ^ BOINCstats - Rosetta@home overview Retrieved on July 1, 2008
- ^ What is Rosetta@home? Introductory overview of Rosetta@home from the project website
- ^ a b BOINC client download List of previous, recommended, and development versions for all available platforms. Also links to third-party distributions for other platforms.
- ^ Rosetta@home recommended system requirements
- ^ Rosetta@home: News. See also Rosetta@home: News archive
- ^ RCSB Protein Data Bank. "Growth of Released Structures Per Year By Molecular Type: Protein Only".
{{cite web}}
: Unknown parameter|accessdaymonth=
ignored (help); Unknown parameter|accessyear=
ignored (|access-date=
suggested) (help) - ^ Bradley; et al. (2005). "Toward high-resolution de novo structure prediction for small proteins". Science. 309 (5742): 638–642. doi:10.1126/science.1113801.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Wang; et al. (2005). "Improved side-chain modeling for protein–protein docking". Protein Science. 14 (5): 1328–1339. doi:10.1110/ps.041222905.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Gray; et al. (2003). "Protein–Protein Docking with Simultaneous Optimization of Rigid-body Displacement and Side-chain Conformations". Journal of Molecular Biology. 331 (1): 281–299. doi:10.1016/S0022-2836(03)00670-3.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Schueler-Furman; et al. (2005). "Progress in protein-protein docking: Atomic resolution predictions in the CAPRI experiment using RosettaDock with an improved treatment of side-chain flexibility". Proteins. 60 (2): 187–194. doi:10.1002/prot.20556.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Sprague; et al. "Crystal Structure of the HSV-1 Fc Receptor Bound to Fc Reveals a Mechanism for Antibody Bipolar Bridging". PLoS Biology. 4 (6): e148. doi:10.1371/journal.pbio.0040148.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: unflagged free DOI (link) - ^ "Homing Endonuclease Genes: New Tools for Mosquito Population Engineering and Control".
- ^ Windbichler; et al. (2007). "Homing endonuclease mediated gene targeting in Anopheles gambiae cells and embryos". Nucleic Acids Research. 35 (17): 5922–5933. doi:10.1093/nar/gkm632.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Ashworth; et al. (2006). "Computational redesign of endonuclease DNA binding and cleavage specificity". Nature. 441. doi:10.1038/nature04818.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Lacy; et al. (2005). "A model of anthrax toxin lethal factor bound to protective antigen". Proc. Natl. Acad. Sci. USA. 102 (45): 16409–16414. doi:10.1073/pnas.0508259102.
{{cite journal}}
: Explicit use of et al. in:|author=
(help) - ^ Albrecht; et al. (2007). "Human Monoclonal Antibodies against Anthrax Lethal Factor and Protective Antigen Act Independently To Protect against Bacillus anthracis Infection and Enhance Endogenous Immunity to Anthrax". Infection and Immunity. 75 (11): 5425–5433. doi:10.1128/IAI.00261-07.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)
External links
Related websites
- Rosetta@home official project Website
- RALPH@home is the official alpha test project for Rosetta@home
- David Baker's Rosetta@home journal
- How-To: Join Distributed Computing projects that benefit humanity
- Volunteer@Home.com — All about volunteer computing
- Flash-based BOINC tutorials, how to attach Rosetta@home with BOINC (English, Czech)
- Rosetta@home project stats