Related Experiment Video
Updated: Jun 21, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Incorporating 1H chemical shift determination into 13C-direct detected spectroscopy of intrinsically disordered
Bernie O'Hare1, Alan J Benesi, Scott A Showalter
1Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA. bvo100@psu.edu
Abstract:
Exclusively heteronuclear (13)C-detected NMR spectroscopy of proteins in solution has seen resurgence in the past several years. For disordered or unfolded proteins, which tend to have poor (1)H-amide chemical shift dispersion, these experiments offer enhanced resolution and the possibility of complete heteronuclear resonance assignment at the cost of leaving the (1)H resonances unassigned. Here we report two novel (13)C-detected NMR experiments which incorporate a (1)H chemical shift evolution period followed by (13)C-TOCSY mixing for aliphatic (1)H resonance assignment without reliance on (1)H detection.
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