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Protein Folding Studied by Dissolution Dynamic Nuclear Polarization

Authors

  • Hsueh-Ying Chen,

    1. Department of Chemistry, Texas A&M University, College Station, TX 77843 (USA)
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    • These authors contributed equally to this work.

  • Mukundan Ragavan,

    1. Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843 (USA)
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    • These authors contributed equally to this work.

  • Prof. Dr. Christian Hilty

    Corresponding author
    1. Department of Chemistry, Texas A&M University, College Station, TX 77843 (USA)
    • Department of Chemistry, Texas A&M University, College Station, TX 77843 (USA)

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  • Financial support from the National Science Foundation (Grants CHE-0846402 and CHE-0840464), the Welch Foundation (Grant A-1658), and Texas A&M University is acknowledged. We thank Prof. Dr. Mikael Oliveberg, Stockholm University for providing the plasmid containing the gene for L23, and Prof. Dr. François Gabbaï for use of the fluorimeter.

Abstract

original image

Folding and hyperpolarization: A method is presented for the measurement of protein folding by nuclear magnetic resonance. Denatured polypeptide is hyperpolarized using dissolution dynamic nuclear polarization, yielding a substantial signal enhancement that allows real-time 13C NMR spectroscopy of the refolding process after a rapid pH jump. The resulting spectra indicate global and site-specific changes in the protein.

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