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NMR methods for investigating functionally relevant biomolecular dynamics
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DOI：10.1016/j.mrl.2025.200195.png)
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Abstract
En 中文
The dynamics of biomolecules span across a wide range of timescales, reflecting the complexity of free energy landscapes of biomolecules. Among these, the microsecond-to-millisecond (mu s-ms) timescale dynamics are particularly significant, offering detailed insights into the kinetic, thermodynamic, and structural aspects of biological function. Many critical biological processes, including enzyme catalysis, protein folding, ligand binding, and allosteric regulation, operate within this timescale. Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for probing molecular dynamics in this time window, commonly used NMR methods for investigating mu s-ms timescale dynamics include Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion, chemical exchange saturation transfer (CEST), and rotating-frame longitudinal relaxation dispersion (R1r relaxation dispersion). This review provides a brief overview of the fundamental principles and some recent advances of these methods, highlighting their interrelationships and applications in elucidating biomolecular dynamics. (c) 2025 The Authors. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co. Ltd. This is an open access article under the CC BY-NC-ND license (http:// creativecommons.org/licenses/by-nc-nd/4.0/).
Keywords:
NMR spectroscopy
Biomolecular dynamics
Conformational exchange
Invisible excited states
CPMG
CEST
Rotating-frame relaxation
Relaxation dispersion
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