Related Experiment Video
Updated: Aug 14, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
Published on: April 19, 2021
13C/15N distance determination by CPMAS NMR in uniformly 13C labeled molecules
Maggy Hologne1, Jésus Raya, Jérôme Hirschinger
1Institut de Chimie, FRE 2446 CNRS, Université Louis Pasteur, BP 296, 67008 Strasbourg Cedex, France.
Abstract:
The REDOR and CPMAS techniques are applied for measuring 13C-15N dipolar coupling constants in glycine. It is shown that the selective CP or SPECIFIC CP technique removes the coherent evolution of the spin system under homonuclear 13C-13C J couplings. While the large coupling constant (approximately 900 Hz) is readily determined because of the presence of large oscillations in the CPMAS dynamics, their absence precludes the measurement of the small coupling constant (approximately 200 Hz). The experimental results and numerical simulations demonstrate that the determination of 13C-15N coupling constants of medium size (<1 kHz) by the CPMAS technique is mainly limited by the strength of the 1H decoupling field and the size of the 13C and 15N chemical shift anisotropies.
Related Concept Videos
Carbon-13 (¹³C) NMR: Overview
¹³C NMR: ¹H–¹³C Decoupling
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
NMR Spectroscopy Of Amines

