Abstract
INTRODUCTION. Genome sequencing projects have already determined nearly complete genome sequences of several organisms, including human. The products of these genes are widely recognized as the next generation of therapeutics and targets for the development of pharmaceuticals. While identification of these genes is proceeding quickly, elucidation of their three-dimensional (3D) structures and biochemical functions lags far behind. In some cases, knowledge of 3D structures of proteins can provide important insights into evolutionary relationships that are not easily recognized by sequence alignment comparisons. Thus, structure determination by NMR or X-ray crystallography can sometimes provide key information regarding protein fold class, locations and clustering of conserved residues, and surface electrostatic field distributions that connect a protein sequence with potential biochemical functions. The resulting limited set of putative biochemical functions can then be tested by appropriate biochemical assays.
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