With the aid of more than 150,000 home computer users throughout the world, Howard Hughes Medical Institute (HHMI) researchers have, for the first time, accurately predicted the three-dimensional structure of a small, naturally occurring globular protein using only its amino acid sequence. The accomplishment was achieved with a newly refined computational method for predicting protein structure, which the researchers say can also improve the detail and accuracy of protein structures generated with experimental techniques.

A detailed understanding of a protein’s structure can offer scientists a wealth of information - revealing intricacies about the protein’s biological function and suggesting new ideas for drug design. Researchers often rely on x-ray crystallography to determine a protein’s structure - bombarding the molecule with x-rays and analyzing the resulting diffraction pattern to piece together its structure. But not all proteins are amenable to this time-consuming technique, and those that are do not always yield the atomic-level data researchers would like to have.
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The complex algorithms the researchers developed to carry out these analyses demand a tremendous amount of computing power. More than 150,000 home computer users around the world were an integral part of the project, volunteering their computers to participate in the quest for protein structures through Rosetta@home, a distributed computing project that is based on the Berkeley Open Infrastructure for Network Computing (BOINC) platform.