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The matrix refolded

Nature Methods volume 2, page 3 (2005)Cite this article

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The postgenomic era has lead to an explosion in protein expression and structural initiatives, from both a biotechnology and an academic perspective1,2. One of the most time- and cost-effective means of producing recombinant proteins uses genetically modified bacteria. A substantial hindrance to these efforts is the formation of insoluble inclusion bodies. In one study, only 13% of the human proteins tested could be purified from bacteria in soluble form3. To obtain native protein, it is necessary to purify inclusion bodies and subsequently solubilize them with denaturing agents. It is generally assumed that there is no one way to treat inclusion bodies and that a series of trial-and-error renaturation experiments must be performed. Identifying the optimal refolding conditions and methodology is therefore rate limiting. A wide range of protein refolding methodologies has been developed, using simple dilution as well as more complex matrix-assisted methods and the addition of solutes to renaturing buffers4,5,6.

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Figure 1: The Refold Database

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Faculty of Medicine and Victorian Bioinformatics Consortium, Monash University, Clayton Campus, Victoria, 3800, Australia

    Ashley M Buckle, Glyn L Devlin, Rachel A Jodun, Kate F Fulton, Noel Faux, James C Whisstock & Stephen P Bottomley

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  1. Ashley M Buckle
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  2. Glyn L Devlin
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  3. Rachel A Jodun
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  4. Kate F Fulton
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  6. James C Whisstock
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  7. Stephen P Bottomley
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Buckle, A., Devlin, G., Jodun, R. et al. The matrix refolded. Nat Methods 2, 3 (2005). https://doi.org/10.1038/nmeth0105-3

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