Protein melts

A new phase for protein chemistry

Proteins are most at home in water, although it has been known for some time that they can remain functional in non-aqueous environments. Researchers have now shown that in solvent-free melts, the oxygen-binding protein myoglobin adopts a near-native structure and retains its biological activity.

Access options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

Figure 1: Chemical modification and polymer conjugation of myoglobin to produce a solvent-free protein–polymer melted phase.

References

  1. 1

    The Molecular Basis of Life: Is Life Possible Without Water? Phil. Trans. R. Soc. Lond. B 359, (special issue) 1143–1328 (2004).

  2. 2

    Klibanov, A. M. Nature 409, 241–246 (2001).

    CAS  Article  Google Scholar 

  3. 3

    Mesiano, A. J., Beckman, E. J. & Russell, A. J. Chem. Rev. 99, 623–633 (1999).

    CAS  Article  Google Scholar 

  4. 4

    Lamare, S. & Legoy, M-D. Trends Biotechnol. 11, 413–418 (1993).

    CAS  Article  Google Scholar 

  5. 5

    Wangikar, P. P., Michels, P. C., Clark, D. S. & Dordick, J. S. J. Am. Chem. Soc. 119, 70–76 (1997).

    CAS  Article  Google Scholar 

  6. 6

    Baross, J. A. et al. The Limits of Organic Life in Planetary Systems (National Acad. Press, 2007).

    Google Scholar 

  7. 7

    Perriman, A. W. et al. Nature Chem. 2, 622–626 10.1038/nchem.700 (2010).

    CAS  Article  Google Scholar 

Download references

Author information

Affiliations

Authors

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Clark, D. A new phase for protein chemistry. Nature Chem 2, 607–608 (2010). https://doi.org/10.1038/nchem.746

Download citation