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Dynamic Nuclear Polarization of Sedimented Solutes

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    Dynamic Nuclear Polarization of Sedimented Solutes
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    § ⊥ §Department of Chemistry “Ugo Schiff” and ⊥Magnetic Resonance Center (CERM), University of Florence, 50019 Sesto Fiorentino (FI), Italy
    ∥ Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States
    [email protected]
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2013, 135, 5, 1641–1644
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    https://doi.org/10.1021/ja312553b
    Published January 18, 2013
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    Abstract

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    Using the 480 kDa iron-storage protein complex, apoferritin (ApoF), as an example, we demonstrate that sizable dynamic nuclear polarization (DNP) enhancements can be obtained on sedimented protein samples. In sedimented solute DNP (SedDNP), the biradical polarizing agent is co-sedimented with the protein, but in the absence of a glass-forming agent. We observe DNP enhancement factors ε > 40 at a magnetic field of 5 T and temperatures below 90 K, indicating that the protein sediment state is “glassy” and suitable to disperse the biradical polarizing agent upon freezing. In contrast, frozen aqueous solutions of ApoF yield ε ≈ 2. Results of SedDNP are compared to those obtained from samples prepared using the traditional glass-forming agent glycerol. Collectively, these and results from previous investigations suggest that the sedimented state can be functionally described as a “microcrystalline glass” and in addition provide a new approach for preparation of samples for DNP experiments.

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    Experimental details for sample preparation and DNP NMR experiments. This material is available free of charge via the Internet at http://pubs.acs.org.

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    This article is cited by 57 publications.

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    Cite this: J. Am. Chem. Soc. 2013, 135, 5, 1641–1644
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja312553b
    Published January 18, 2013
    Copyright © 2013 American Chemical Society
    Request reuse permissions

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