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Journal Article

Hyperpolarized binding pocket nuclear Overhauser effect for determination of competitive ligand binding

MPS-Authors
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Mazur,  A.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Wegstroh,  M.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Reese,  M.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lee,  D.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Supplementary Material (public)

1478442_sm_miscellaneous_information.pdf
(Supplementary material), 778KB

Citation

Lee, Y., Zeng, H., Mazur, A., Wegstroh, M., Carlomagno, T., Reese, M., et al. (2012). Hyperpolarized binding pocket nuclear Overhauser effect for determination of competitive ligand binding. Angewandte Chemie International Edition, 51(21), 5179-5182. doi:10.1002/anie.201201003.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-9E66-4
Abstract
Protein-mediated polarization transfer: Ligands L1 and L2 that competitively bind to a protein are subject to indirect spin-polarization transfer through the binding site of the protein. If protons HL1 of one ligand are hyperpolarized by dynamic nuclear polarization (DNP, see picture), signal intensities in the NMR spectrum of the second ligand become enhanced. The relative build-up of signal of the second ligand yields information on its binding epitope.