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The explosion in genome sequencing, and the
DNA
array experiments based on those sequences, have provided a wealth of information on gene sequence, organization, and expression. This has led to a desire to carry out similarly broad experiments on all proteins encoded by a genome—the proteome. Although mass spectrometry (MS) is proving to be a powerful tool in the study of proteomes, the information it provides is relatively one-dimensional. The only feasible way to study the rich complexity of protein expression, modification, and interaction on a genomic scale may be to derive well-characterized specific antibodies (or other binding ligands) that recognize each individual protein. Traditional immunization approaches will be unable to generate such banks of antibodies in sufficient quantity, quality, or reproducibility, and as a result, biomolecular-diversity selection methods—such as phage, ribosome, or mRNA display—will probably be used.