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  High-resolution NMR determination of the dynamic structure of membrane proteins.

Jaremko, M., Jaremko, L., Villinger, S., Schmidt, C. D., Griesinger, C., Becker, S., et al. (2016). High-resolution NMR determination of the dynamic structure of membrane proteins. Angewandte Chemie International Edition, 55(35), 101518-10521. doi:10.1002/anie.201602639.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-34DA-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-34E0-B
Genre: Journal Article

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 Creators:
Jaremko, M.1, Author              
Jaremko, L.1, Author              
Villinger, S.1, Author              
Schmidt, C. D.2, Author              
Griesinger, C.2, Author              
Becker, S.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: NMR spectroscopy; membrane proteins; protein dynamics; relaxation; structure determination
 Abstract: (15) N spin-relaxation rates are demonstrated to provide critical information about the long-range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation-rate-derived structure of the 283-residue human voltage-dependent anion channel revealed an anisotropically shaped barrel with a rigidly attached N-terminal helix. Our study thus establishes an NMR spectroscopic approach to determine the structure and dynamics of mammalian membrane proteins at high accuracy and resolution.

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Language(s): eng - English
 Dates: 2016-07-272016-08-22
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201602639
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 55 (35) Sequence Number: - Start / End Page: 101518 - 10521 Identifier: -