NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Angew Chem Int Ed Engl. 2016 Dec 12;55(50):15504-15509. doi: 10.1002/anie.201607084. Epub 2016 Nov 16.


We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100-111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα-Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

Keywords: magic-angle spinning; proton detection; resonance assignment; solid-state NMR spectroscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter / virology
  • Amyloid / chemistry*
  • Animals
  • Bacteriophages / chemistry
  • Crystallization
  • Humans
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Nucleocapsid / chemistry
  • Protein Multimerization
  • Proteins / chemistry*
  • Protons


  • Amyloid
  • Proteins
  • Protons