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Updated: Apr 21, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Triple resonance-based ¹³C(α) and ¹³C(β) CEST experiments for studies of ms timescale dynamics in proteins
Dong Long1, Ashok Sekhar, Lewis E Kay
1Departments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, ON, M5S 1A8, Canada.
Abstract:
A pair of triple resonance based CEST pulse schemes are presented for measuring ¹³C(α) and ¹³C(β) chemical shifts of sparsely populated and transiently formed conformers that are invisible to traditional NMR experiments. CEST profiles containing dips at resonance positions of ¹³C(α) or ¹³C(β) spins of major (ground) and minor (excited) conformers are obtained in a pseudo 3rd dimension that is generated by quantifying modulations of cross peaks in ¹⁵N, ¹H(N) correlation spectra. An application to the folding reaction of a G48A mutant of the Fyn SH3 domain is presented, illustrating and validating the methodology.
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