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

Angew Chem Int Ed Engl. 2016 Aug 22;55(35):10518-21. doi: 10.1002/anie.201602639. Epub 2016 Jul 27.


(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.

Keywords: NMR spectroscopy; membrane proteins; protein dynamics; relaxation; structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Membrane Proteins / chemistry*
  • Molecular Dynamics Simulation*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Conformation


  • Membrane Proteins