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100 1 _ |a Viennet, Thibault
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245 _ _ |a Selective Protein Hyperpolarization in Cell Lysates Using Targeted Dynamic Nuclear Polarization
260 _ _ |a Weinheim
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520 _ _ |a Nuclear magnetic resonance (NMR) spectroscopy has the intrinsic capabilities to investigate proteins in native environments. In general, however, NMR relies on non-natural protein purity and concentration to increase the desired signal over the background. We here report on the efficient and specific hyperpolarization of low amounts of a target protein in a large isotope-labeled background by combining dynamic nuclear polarization (DNP) and the selectivity of protein interactions. Using a biradical-labeled ligand, we were able to direct the hyperpolarization to the protein of interest, maintaining comparable signal enhancement with about 400-fold less radicals than conventionally used. We could selectively filter out our target protein directly from crude cell lysate obtained from only 8 mL of fully isotope-enriched cell culture. Our approach offers effective means to study proteins with atomic resolution in increasingly native concentrations and environments.
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700 1 _ |a Viegas, Aldino
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700 1 _ |a Kuepper, Arne
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700 1 _ |a Arens, Sabine
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700 1 _ |a Gelev, Vladimir
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700 1 _ |a Petrov, Ognyan
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700 1 _ |a Grossmann, Tom N.
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700 1 _ |a Heise, Henrike
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700 1 _ |a Etzkorn, Manuel
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773 _ _ |a 10.1002/anie.201603205
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