Protein improvement strategies today involve widely varying combinations of rational design with random mutagenesis and screening. To make further progress—defined as making subsequent protein engineering problems easier to solve—protein engineers must critically compare these strategies and eliminate less effective ones.
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References
Lutz, S. & Bornscheuer, U.T. (eds.). Protein Engineering Handbook (Wiley-VCH, Weinheim, 2009).
Estell, D.A., Graycar, T.P. & Wells, J.A. J. Biol. Chem. 260, 6518–6521 (1985).
Fox, R.J. et al. Nat. Biotechnol. 25, 338–344 (2007).
Gray, K.A., Zhao, L. & Emptage, M. Curr. Opin. Chem. Biol. 10, 141–146 (2006).
McCarthy, A. Chem. Biol. 10, 893–894 (2003).
Eschenmoser, A. & Wintner, C.E. Science 196, 1410–1420 (1977).
Woodward, R.B. Pure Appl. Chem. 33, 145–177 (1973).
Chen-Goodspeed, M., Sogorb, M.A., Wu, F. & Raushel, F.M. Biochemistry 40, 1332–1339 (2001).
Seelig, B. & Szostak, J.W. Nature 448, 828–831 (2007).
Qian, Z. & Lutz, S. J. Am. Chem. Soc. 127, 13466–13467 (2005).
Morley, K.L. & Kazlauskas, R.J. Trends Biotechnol. 23, 231–237 (2005).
Neylon, C. Nucleic Acids Res. 32, 1448–1459 (2004).
Carr, R. et al. ChemBioChem 6, 637–639 (2005).
DeSantis, G. et al. J. Am. Chem. Soc. 125, 11476–11477 (2003).
Bloom, J.D., Labthavikul, S.T., Otey, C.R. & Arnold, F.H. Proc. Natl. Acad. Sci. USA 103, 5869–5874 (2006).
Weinreich, D.M., Delaney, N.F., DePristo, M.A. & Hartl, D.L. Science 312, 111–114 (2006).
Reetz, M.T. & Sanchis, J. ChemBioChem 9, 2260–2267 (2008).
Whittle, E. & Shanklin, J. J. Biol. Chem. 276, 21500–21505 (2001).
Reetz, M.T., Wang, L.W. & Bocola, M. Angew. Chem. Int. Ed. 45, 1236–1241 (2006).
Reetz, M.T., Kahakeaw, D. & Lohmer, R. ChemBioChem 9, 1797–1804 (2008).
Bloom, J.D., Romero, P.A., Lu, Z. & Arnold, F.H. Biol. Direct 2, 17 (2007).
Gupta, R.D. & Tawfik, D.S. Nat. Methods 5, 939–942 (2008).
Stemmer, W.P. Nature 370, 389–391 (1994).
Acknowledgements
U.T.B. thanks the German Research Foundation (DFG, Grant Bo1862/4-1) and R.J.K. the US National Science Foundation (CHE-0616560) for financial support.
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Kazlauskas, R., Bornscheuer, U. Finding better protein engineering strategies. Nat Chem Biol 5, 526–529 (2009). https://doi.org/10.1038/nchembio0809-526
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DOI: https://doi.org/10.1038/nchembio0809-526
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