Double-nucleus enhanced recoupling for efficient 13C MAS NMR correlation spectroscopy of perdeuterated proteins

J Am Chem Soc. 2009 Dec 2;131(47):17054-5. doi: 10.1021/ja907493p.

Abstract

The use of both proton and deuterium dipolar coupling networks to obtain efficient (13)C magic-angle-spinning NMR correlation spectroscopy is introduced. This new strategy aims to improve the efficiency of (13)C spin diffusion in perdeuterated proteins. The method is called double-nucleus enhanced recoupling (DONER), and it provides significantly improved transfer efficiency for carbon spin diffusion at low proton density. The C(alpha) cross-peak intensity in the DONER experiment is approximately 3 and approximately 5 times stronger than those in conventional radio-frequency-assisted diffusion (RAD) and proton-driven spin diffusion (PDSD) experiments, respectively. Remarkably, the full cross-peak pattern for the aliphatic region of an extensively perdeuterated SH3 protein sample can be obtained using the DONER approach with direct (13)C excitation.

MeSH terms

  • Deuterium / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation
  • Proteins / chemistry*

Substances

  • Proteins
  • Deuterium