Double-nucleus enhanced recoupling for efficient 13C MAS NMR correlation spectroscopy of perdeuterated proteins.
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.
Akbey
Umit
U
Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rossle-Str. 10, 13125 Berlin, Germany.
Oschkinat
Hartmut
H
van Rossum
Barth-Jan
BJ
D003903:Deuterium / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins; D003903:Deuterium