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Updated: May 2, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Ultrafast two-dimensional NMR relaxometry for investigating molecular processes in real time
Susanna Ahola1, Ville-Veikko Telkki
1Department of Physics, NMR Research Group, University of Oulu, P.O.Box 3000, FIN-90014 (Finland).
Abstract:
Nuclear spin-lattice (T1) and spin-spin (T2) relaxation times provide versatile information about the dynamics and structure of substances, such as proteins, polymers, porous media, and so forth. Multidimensional experiments increase the information content and resolution of NMR relaxometry, but they also multiply the measurement time. To overcome this issue, we present an efficient strategy for a single-scan measurement of a 2D T1-T2 correlation map. The method shortens the experimental time by one to three orders of magnitude as compared to the conventional method, offering an unprecedented opportunity to study molecular processes in real-time. We demonstrate that, despite the tremendous speed-up, the T1-T2 correlation maps determined by the single-scan method are in good agreement with the maps measured by the conventional method. The concept of the single-scan T1-T2 correlation experiment is applicable to a broad range of other multidimensional relaxation and diffusion experiments.
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