Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR

Structure. 2012 Jun 6;20(6):1019-27. doi: 10.1016/j.str.2012.03.010. Epub 2012 May 3.


Nuclear magnetic resonance (NMR) structure calculations of the α-helical integral membrane proteins DsbB, GlpG, and halorhodopsin show that distance restraints from paramagnetic relaxation enhancement (PRE) can provide sufficient structural information to determine their structure with an accuracy of about 1.5 Å in the absence of other long-range conformational restraints. Our systematic study with simulated NMR data shows that about one spin label per transmembrane helix is necessary for obtaining enough PRE distance restraints to exclude wrong topologies, such as pseudo mirror images, if only limited other NMR restraints are available. Consequently, an experimentally realistic amount of PRE data enables α-helical membrane protein structure determinations that would not be feasible with the very limited amount of conventional NOESY data normally available for these systems. These findings are in line with our recent first de novo NMR structure determination of a heptahelical integral membrane protein, proteorhodopsin, that relied extensively on PRE data.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Computer Simulation
  • DNA-Binding Proteins / chemistry*
  • Endopeptidases / chemistry*
  • Escherichia coli Proteins / chemistry*
  • Halorhodopsins / chemistry*
  • Hydrogen Bonding
  • Membrane Proteins / chemistry*
  • Models, Molecular*
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Bacterial Proteins
  • DNA-Binding Proteins
  • DsbB protein, Bacteria
  • Escherichia coli Proteins
  • GlpG protein, E coli
  • Halorhodopsins
  • Membrane Proteins
  • Endopeptidases