Homology modeling (also known as comparative modeling) is, to date, the most reliable and well-established computational approach for predicting protein structures. In this method, one or more experimental three-dimensional structures of related homologous proteins are identified and used as templates, based on which an atomic-resolution model of the "target" protein is built from its amino acid sequence. It has been shown that three-dimensional protein structure is evolutionarily more conserved than would be expected on the basis of sequence conservation alone. Thus, even proteins that have diverged appreciably in sequence but still share detectable similarity will also share common structural properties, particularly the overall folding.
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Bacteria are the most widely used protein expression systems in which fast production of recombinant proteins has been achieved due to their rapid growth, high yields, simple culture conditions and ease of scale-up. Bacterial expression systems also feature low production costs and high scalability, making them an attractive option for recombinant protein production.
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