TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding

Methods Mol Biol. 2004:278:161-84. doi: 10.1385/1-59259-809-9:161.

Abstract

Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.

MeSH terms

  • Hydrogen Bonding
  • Macromolecular Substances
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Nucleic Acids / chemistry
  • Proteins / chemistry*

Substances

  • Macromolecular Substances
  • Nucleic Acids
  • Proteins