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Updated: May 31, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Exchange enhanced sensitivity gain for solvent-exchangeable protons in 2D 1H-15N heteronuclear correlation spectra
Shenggen Yao1, Mark G Hinds, James M Murphy
1The Walter & Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3052, Australia. syao@wehi.edu.au
Abstract:
Conformational or chemical exchange can cause significant sensitivity loss in NMR spectroscopy through resonance broadening for nuclear spins involved in these processes. While this effect may sometimes be alleviated by manipulating experimental conditions such as temperature, pH, and buffers, conditions optimal for all resonances are not always achievable. As a consequence, any means of recovering or minimizing this exchange-induced sensitivity loss is potentially of significant value in regaining information otherwise lost. We report the experimental observation of significant sensitivity gain for nuclear spins undergoing chemical exchange with solvent (water) at exchange rates ca 1-10 s(-1) in (1)H-(15)N correlation spectra of proteins acquired with band-selective pulses (the SOFAST-HMQC sequence).
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