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Structural genomics
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== Goals== One goal of structural genomics is to identify novel protein folds. Experimental methods of protein structure determination require proteins that express and/or crystallize well, which may inherently bias the kinds of proteins folds that this experimental data elucidate. A genomic, modeling-based approach such as [[de novo protein structure prediction|''ab initio'' modeling]] may be better able to identify novel protein folds than the experimental approaches because they are not limited by experimental constraints. Protein function depends on 3-D structure and these 3-D structures are more highly conserved than [[peptide sequence|sequences]]. Thus, the high-throughput structure determination methods of structural genomics have the potential to inform our understanding of protein functions. This also has potential implications for drug discovery and protein engineering.<ref>{{cite journal |vauthors=Kuhn P, Wilson K, Patch MG, Stevens RC |title=The genesis of high-throughput structure-based drug discovery using protein crystallography |journal=Curr Opin Chem Biol |volume=6 |issue=5 |pages=704β10 |date=October 2002 |pmid=12413557 |doi=10.1016/S1367-5931(02)00361-7}}</ref> Furthermore, every protein that is added to the structural database increases the likelihood that the database will include homologous sequences of other unknown proteins. The [[Protein Structure Initiative]] (PSI) is a multifaceted effort funded by the [[National Institutes of Health]] with various academic and industrial partners that aims to increase knowledge of protein structure using a structural genomics approach and to improve structure-determination methodology.
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