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Ironing out the protein folding problem?

Nature Biotechnology volume 17, pages 136–137 (1999)Cite this article

Folding an isolated or expressed globular protein is a major biotechnological problem and often limits the commercialization of protein–based therapeutics. In this issue, Alan Fersht and colleagues1 present a potential solution, using a biomimetic approach that exploits elements of the cellular machinery to fold proteins in vitro. Their work involves the application of several immobilized reagents that are designed to prevent aggregation and avoid kinetic traps of incorrect disulfide pairing and/or incorrect isomers of peptide bonds involving proline.

Try to refold a new shirt to its packaged form after you've tried it on, and you'll have a vague idea of the problem that a protein may have in adopting what is known as its native structure. The amino acid sequence that defines a particular protein must fold to a specific conformation to be biologically active. Unlike haberdashery, the information for this three–dimensional structure is conveniently contained within the one–dimensional sequence of amino acids, and proteins usually fold with high efficiency within cells.

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Figure 1: Untangling the paths of protein folding.

References

  1. Altamirano, M.M. et al. 1999. Nat. Biotechnol. 17:187–191.

    Article  CAS  Google Scholar 

  2. Kane, J.F. and Hartley, D.L. 1988. Trends Biotechnol. 6:95–100.

    Article  CAS  Google Scholar 

  3. Jaenicke, R. 1987. Prog. Biophys. Mol. Biol. 49:117–237.

    Article  CAS  Google Scholar 

  4. Fisher, G. and Schmid, F.X. 1990. Biochemistry 29:2205–2215.

    Article  Google Scholar 

  5. Gething, M.J. and Sambrook, J. 1992. Nature 355:33–45.

    Article  CAS  Google Scholar 

  6. Zardenta, G. and Horowitz, P.M. 1994. Anal. Biochem. 223:1–6.

    Article  Google Scholar 

  7. Sigler, P.B. et al. 1998. Annu. Rev. Biochem. 67:581–608.

    Article  CAS  Google Scholar 

  8. Zahn, R. et al. 1996. Proc. Natl. Acad. Sci. USA 93:15024–15029.

    Article  CAS  Google Scholar 

  9. Anfinson, C. et al. (eds.). 1993. Accessory folding proteins. Academic Press, New York.

    Google Scholar 

  10. Horowitz, P.M. and Simon, D. 1986. J. Biol. Chem. 261:13887–13891.

    CAS  PubMed  Google Scholar 

Download references

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  1. professor at the department of biochemistry, University of Texas Health Science Center at San Antonio, 7703 Floyd Carl Dr., San Antonio, 78284, TX

    Paul M. Horowitz

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  1. Paul M. Horowitz
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Horowitz, P. Ironing out the protein folding problem?. Nat Biotechnol 17, 136–137 (1999). https://doi.org/10.1038/6136

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