High-dimensional NMR spectra for structural studies of biomolecules

Chemphyschem. 2013 Sep 16;14(13):3015-25. doi: 10.1002/cphc.201300277. Epub 2013 Jun 21.

Abstract

Recent developments in the acquisition and processing of NMR data sets facilitate the recording of ultra-high-resolution NMR spectra in a reasonable time. The new experiments allow easy resonance assignment for folded and unfolded proteins, as well as the precise determination of spectral parameters, for example, chemical shifts, NOE contacts, coupling constants or cross-correlated relaxation rates. Owing to exceptional resolution of 4D-6D spectroscopy, detailed studies of biomolecules of unprecedented complexity are now possible. Herein, the principles of acquisition and processing methods are presented. The main applications of high-dimensional NMR experiments, including backbone and side-chain resonance assignment in proteins, as well as heteronuclear edited NOE techniques are reviewed.

Keywords: NMR spectroscopy; bioorganic chemistry; nonuniform sampling; proteins; sparse sampling.

Publication types

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

MeSH terms

  • Magnetic Resonance Spectroscopy / methods*
  • Proteins / chemistry*

Substances

  • Proteins