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Biological Chemistry

Baker's yeast proteins analyzed

March 26, 2007 | APPEARED IN VOLUME 85, ISSUE 13

It would be nice to know the structures of all biological proteins because structure begets function. But in organisms like yeast, the structures and functions of most proteins are unknown. Now, David Baker of the University of Washington, Seattle, and coworkers have predicted the structures of most previously uncharacterized yeast proteins in one swoop (PLoS Biol., DOI: 10.1371/journal.pbio.0050076). The researchers used their de novo structure-prediction program, Rosetta, and distributed computing to estimate the structures of thousands of domains from the proteins. They then used experimental data on yeast protein function and localization to refine the predictions and assigned many of the domains to protein superfamilies. Most superfamilies have one or just a few molecular functions, so the assignments suggest likely functions. "Future work will include an ongoing effort to scale this procedure to over 150 completely sequenced genomes" and the use of higher resolution structure-prediction methods, the researchers note.

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