Hidden Motions and Motion-Induced Invisibility: Dynamics-based Spectral Editing in Solid-State NMR

Methods. 2018 Sep 15;148:123-135. doi: 10.1016/j.ymeth.2018.04.015. Epub 2018 Apr 24.


Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids. Such biological samples feature functionally relevant molecular dynamics, which often affect different parts of the sample in different ways. Solid-state NMR experiments' sensitivity to dynamics represents a double-edged sword. On the one hand, it offers a chance to measure dynamics in great detail. On the other hand, certain types of motion lead to signal loss and experimental inefficiencies that at first glance interfere with the application of ssNMR to overly dynamic proteins. Dynamics-based spectral editing (DYSE) ssNMR methods leverage motion-dependent signal losses to simplify spectra and enable the study of sub-structures with particular motional properties.

Keywords: Dynamics; Membrane proteins; Protein aggregation; Solid-state NMR; Structural biology.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

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


  • Membrane Proteins