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Protein engineering 20 years on

Nature Reviews Molecular Cell Biology volume 3, pages 964–970 (2002)Cite this article

Abstract

It is 20 years since site-directed mutagenesis was first used to modify the active site of an enzyme of known structure and mechanism. Since then, this method has contributed far-reaching insights into catalysis, specificity, stability and folding of proteins. Engineered proteins are now being used in industry and for the improved treatment of human disease.

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Figure 1: The active site of tyrosyl–transfer RNA synthetase.
Figure 2: Oxygen saturation curves for haemoglobin.
Figure 3: Ribbon diagrams of insulin.

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Acknowledgements

We thank G. Winter for his critical comments and helpful advice, and the Wellcome Trust and the Biotechnology and Biological Sciences Research Council for supporting our research.

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Authors and Affiliations

  1. the Department of Chemistry, Structural Biology Laboratory, University of York, York, YO10 5YW, UK

    James A. Brannigan & Anthony J. Wilkinson

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  1. James A. Brannigan
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Correspondence to James A. Brannigan or Anthony J. Wilkinson.

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DATABASES

Swiss-Prot

β-lacatamse

insulin

lysozyme

myoglobin

TyrRS

FURTHER INFORMATION

York Structural Biology Laboratory

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Brannigan, J., Wilkinson, A. Protein engineering 20 years on. Nat Rev Mol Cell Biol 3, 964–970 (2002). https://doi.org/10.1038/nrm975

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