Structural genomics

Related to the discipline of proteomics is that of structural genomics. The latter focuses upon the large-scale systematic study of gene product structure. While this embraces rRNA and tRNA, in practice the field focuses upon protein structure. The basic approach to structural genomics entails the cloning and recombinant expression of cellular proteins, followed by their purification and three-dimensional structural analysis. High-resolution determination of a protein's structure is amongst the most challenging of molecular investigations. By the year 2000, protein structure databanks housed in the region of 12 000 entries. However, such databanks are highly redundant, often containing multiple entries describing variants of the same molecule. For example, in excess of 50 different structures of 'insulin' have been deposited (e.g. both native and mutated/engineered forms from various species, as well as insulins in various polymeric forms and in the presence of various stabilizers and other chemicals). In reality, by the year 2000, the three-dimensional structure of approximately 2000 truly different proteins had been resolved.

Until quite recently, X-ray crystallography was the technique used almost exclusively to resolve the three-dimensional structure of proteins. As well as itself being technically challenging, a major limitation of X-ray crystallography is the requirement for the target protein to be in crystalline form. It has thus far proven difficult/impossible to induce the majority of proteins to crystallize. NMR is an analytical technique that can also be used to determine the three-dimensional structure of a molecule, and without the necessity for crystallization. For many years, even the most powerful NMR machines could resolve the three-dimensional structure of only relatively small proteins (less than 20-25 kDa). However, recent analytical advances now render it possible to analyse much larger proteins by this technique successfully.

The ultimate goal of structural genomics is to provide a complete three-dimensional description of any gene product. Also, as the structures of more and more proteins of known function are elucidated, it should become increasingly possible to link specific functional attributes to specific structural attributes. As such, it may prove ultimately feasible to predict protein function if its structure is known, and vice versa.

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