NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond.

Mainz, A.; Religa, T. L.; Sprangers, R.; Linser, R.; Kay, L. E.; Reif, B.

doi:10.1002/anie.201301215

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NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond.

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Linser, R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Mainz, A., Religa, T. L., Sprangers, R., Linser, R., Kay, L. E., & Reif, B. (2013). NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond. Angewandte Chemie International Edition, 52(33), 8746-8751. doi:10.1002/anie.201301215.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0018-9F5E-1

Abstract

Bigger is better: Sequential backbone assignments are obtained by NMR spectroscopy for a 1 MDa proteasome complex. The method relies on immobilization of a soluble protein complex by magic-angle spinning. Deuteration and proton detection of exchangeable sites and paramagnetic relaxation enhancement enables exploration of structural and dynamic properties of supramolecular assemblies at atomic resolution.