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Updated: Jun 18, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Double-nucleus enhanced recoupling for efficient 13C MAS NMR correlation spectroscopy of perdeuterated proteins
Umit Akbey1, Hartmut Oschkinat, Barth-Jan van Rossum
1Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rossle-Str. 10, 13125 Berlin, Germany.
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.
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