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  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. (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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-9F5E-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C5BB-D
Genre: Journal Article

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1977448.pdf (Publisher version), 3MB
 
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 Creators:
Mainz, A., Author
Religa, T. L., Author
Sprangers, R., Author
Linser, R.1, Author              
Kay, L. E., Author
Reif, B., Author
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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Free keywords: magic-angle spinning; molecular weight limit; NMR spectroscopy; proteins; sedimentation
 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.

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Language(s): eng - English
 Dates: 2013-07-192013-08-12
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201301215
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Title: Angewandte Chemie International Edition
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Source Genre: Journal
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Pages: - Volume / Issue: 52 (33) Sequence Number: - Start / End Page: 8746 - 8751 Identifier: -