High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins

Mariusz Jaremko, Łukasz Jaremko, Saskia Villinger, Christian D. Schmidt, Christian Griesinger, Stefan Becker, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


15N 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.

Original languageEnglish (US)
Pages (from-to)10518-10521
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number35
StatePublished - Aug 22 2016
Externally publishedYes

Bibliographical note

Funding Information:
M. and Ł. Jaremko would like to thank Prof. Andrzej Ejchart for sharing his time and expertise about nuclear magnetic relaxation. We thank R. Briones and B.L. de Groot for the MD coordinates. This work was supported by a Fonds der Chemischen Industrie scholarship (to S.V.) and the Deutsche Forschungsgemeinschaft (DFG) collaborative research center SFB803 (to C.G. and M.Z.), and the ERC Grant Agreement 282008 (to M.Z.) and the Erwin Neher Nobel Fellowship (to M.J.). The NMR ensemble of E73V hVDAC1 refined against the R

Publisher Copyright:
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim


  • NMR spectroscopy
  • membrane proteins
  • protein dynamics
  • relaxation
  • structure determination

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)


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