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The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding

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Abstract

The folding of proteins that contain disulfide bonds is termed oxidative protein folding. It involves a chemical reaction resulting in the formation of disulfide bonds and a physical conformational folding reaction that promotes the formation of the native structure. While the presence of disulfide bonds significantly increases the complexity of the folding landscape, it is generally recognized that native disulfide bonds help funnel the trajectory towards the final folded form. Here, we review the role of disulfide bonds in oxidative protein folding and argue that even structure-inducing native disulfide bond formation treads a fine line in the regeneration of disulfide-bond-containing proteins. The translation of this observation to protein misfolding related disorders is discussed.

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Acknowledgements

The author would like to thank Mr. Gyan M. Narayan for assistance with the References.

Funding

MN acknowledges support from NIH 1SC3 GM111200 01A1 for this work. The authors declare no competing financial interests.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, The University of Texas at El Paso (UTEP), 500 W. University Ave., El Paso, TX, 79968, USA

    Mahesh Narayan

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  1. Mahesh Narayan
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MN conceived the topic and wrote the manuscript.

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Correspondence to Mahesh Narayan.

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Narayan, M. The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding. Protein J 40, 134–139 (2021). https://doi.org/10.1007/s10930-021-09976-7

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