High-throughput gene sequencing efforts have been so successful, that now hundreds of thousands of gene sequences for proteins reside in public and private databases. The trick now is to discover the functions of these novel proteins. Unfortunately, sequences represent linear strings of amino acids that contain limited information. Proteins fold up into complex three dimensional structures sporting helixes, loops, strands, and coils. These structures determine a protein's activity. While it is assumed that the sequences contain the rules for how particular proteins naturally fold into different conformations, scientists don't yet know what the rules are. They remain puzzled by "the protein folding problem."
The efforts of thousands of researchers in the past 20 years have yielded structures for about only 20,000 proteins out of 500,000 known protein sequences. Still, when combined with the latest experimental and computational techniques, sequence and structural information provide some useful guidelines. Pharmaceutical companies are using it to sift from massive amounts of sequence information a more manageable number of biologically relevant targets; the undertaking is now known as structural genomics
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