Solid-state Nuclear Magnetic Resonance Structural Studies of Proteins Using Paramagnetic Probes

Solid State Nucl Magn Reson. May-Jun 2012;43-44:1-13. doi: 10.1016/j.ssnmr.2012.02.007. Epub 2012 Mar 9.

Abstract

Determination of three-dimensional structures of biological macromolecules by magic-angle spinning (MAS) solid-state NMR spectroscopy is hindered by the paucity of nuclear dipolar coupling-based restraints corresponding to distances exceeding 5 Å. Recent MAS NMR studies of uniformly (13)C,(15)N-enriched proteins containing paramagnetic centers have demonstrated the measurements of site-specific nuclear pseudocontact shifts and spin relaxation enhancements, which report on electron-nucleus distances up to ~20 Å. These studies pave the way for the application of such long-distance paramagnetic restraints to protein structure elucidation and analysis of protein-protein and protein-ligand interactions in the solid phase. Paramagnetic species also facilitate the rapid acquisition of high resolution and sensitivity multidimensional solid-state NMR spectra of biomacromolecules using condensed data collection schemes, and characterization of solvent-accessible surfaces of peptides and proteins. In this review we discuss some of the latest applications of magic-angle spinning NMR spectroscopy in conjunction with paramagnetic probes to the structural studies of proteins in the solid state.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Electrons
  • Humans
  • Magnetic Phenomena*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Proteins / chemistry*
  • Solvents / chemistry
  • Surface Properties

Substances

  • Proteins
  • Solvents