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Synthetic protein folding

Organic solvent enhances oxidative folding of disulfide-rich proteins

Nature Chemistry (2024)Cite this article

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Natural protein folding takes place in aqueous cell environments. Now, it has been found that proteins in a water-free environment undergo faster and more efficient folding.

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Fig. 1: Ultrafast folding of synthetic microproteins bearing multiple disulfide bonds applying organic media.

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Acknowledgements

N.M. thanks the support from the Israel Science Foundation (1388/22). S.L. thanks the Emergency Postdoctoral Program of the Israel Academy of Sciences and Humanities.

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Authors and Affiliations

  1. Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

    Shay Laps & Norman Metanis

  2. Center for Nanoscience and Nanotechnology, Hebrew University of Jerusalem, Jerusalem, Israel

    Norman Metanis

  3. Casali Center for Applied Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

    Norman Metanis

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  1. Shay Laps
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  2. Norman Metanis
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Correspondence to Norman Metanis.

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Laps, S., Metanis, N. Organic solvent enhances oxidative folding of disulfide-rich proteins. Nat. Chem. (2024). https://doi.org/10.1038/s41557-024-01518-9

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