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Updated: Aug 12, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
Published on: April 19, 2021
Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N
Vitali Tugarinov1, Wing-Yiu Choy, Eriks Kupce
1Protein Engineering Network Centres of Excellence and the Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, M5S lA8, Toronto, Ontario, Canada.
Abstract:
A quantitative analysis of 2D (1)H-(15)N spectra is often complicated by resonance overlap. Here a simple method is presented for resolving overlapped correlations by recording 2D projection planes from HNCO data sets. Applications are presented involving the measurement of (15)N T(1rho) relaxation rates in a high molecular weight protein, malate synthase G, and in a system that exchanges between folded and unfolded states, the drkN SH3 domain. By supplementing relaxation data recorded in the conventional way as a series of 2D (1)H-(15)N data sets with a series of a pair of projection planes the number of dynamics probes is increased significantly for both systems studied.
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