Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations

Biophys J. 2012 Jul 3;103(1):29-37. doi: 10.1016/j.bpj.2012.05.016.


Elemental biological functions such as molecular signal transduction are determined by the dynamic interplay between polypeptides and the membrane environment. Determining such supramolecular arrangements poses a significant challenge for classical structural biology methods. We introduce an iterative approach that combines magic-angle spinning solid-state NMR spectroscopy and atomistic molecular dynamics simulations for the determination of the structure and topology of membrane-bound systems with a resolution and level of accuracy difficult to obtain by either method alone. Our study focuses on the Shaker B ball peptide that is representative for rapid N-type inactivating domains of voltage-gated K(+) channels, associated with negatively charged lipid bilayers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Intracellular Signaling Peptides and Proteins
  • Lipid Bilayers / chemistry
  • Magnetic Resonance Spectroscopy
  • Molecular Dynamics Simulation*
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Potassium Channels, Voltage-Gated / chemistry


  • Intracellular Signaling Peptides and Proteins
  • Lipid Bilayers
  • Peptides
  • Potassium Channels, Voltage-Gated
  • Shaker B inactivating peptide