Conclusions

The growth of genetic engineering in the biotechnology industry offers the promise of the next industrial revolution in the coming decades as artificial proteins are designed for a host of applications and as the properties of wild-type proteins are altered through recombinant experiments. However, the ability to create improved protein products will require considerable guidance from chemical theory to select those mutants most likely to possess the desired functional properties. Molecular mechanics studies of possible mutant proteins will thus become increasingly common in biotechnology. Theoretical molecular design studies, particularly of molecular binding, have already become the principal methods of drug design in the pharmaceutical industry, and they will undoubtedly be widely used in the design of flavorants in the food industry. Other more complicated systems that might be susceptible to molecular design calculations as computers become larger and faster are gelation and textural properties. Computer simulations cannot currently be applied to every practical problem of interest, so care must be exercised in selecting for study those problems for which a well-defined objective might reasonably be accomplished with the resources available. Nevertheless, for those systems for which they are appropriate, theoretical calculations can provide information that is not available by any other technique and can be quite valuable in making the production of functional mutants more efficient.

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