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Folding under the influence

Nature Structural Biology volume 6, pages 304–307 (1999)Cite this article

Abstract

Refolding experiments of acylphosphatase in the presence of trifluoroethanol, a cosolvent known to increase the stability of α-helices, suggest that productive folding depends on optimizing the number of native-like interactions present in the unfolded state.

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Figure 1: Representations47 of a, bovine common type acylphosphatase48 (2ACY) b, horse muscle acylphosphatase49 (model 4 in 1APS) and c, activation domain of human procarboxypeptidase A250 (1AYE).
Figure 2: Refolding of common type AcP in the presence of TFE.

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Acknowledgements

We thank J.A. Zitzewitz for helpful comments on this manuscript.

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Authors and Affiliations

  1. R.M. Ionescu is a postdoctoral fellow and C.R. Matthews is a Professor of Chemistry in the Chemistry Department, Pennsylvania State University, University Park, 16802, Pennsylvania, USA

    Roxana M. Ionescu & C. Robert Matthews

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  1. Roxana M. Ionescu
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  2. C. Robert Matthews
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Correspondence to C. Robert Matthews.

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Ionescu, R., Matthews, C. Folding under the influence. Nat Struct Mol Biol 6, 304–307 (1999). https://doi.org/10.1038/7534

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