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Updated: Jul 3, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
On the origin of NMR dipolar waves in transient helical elements of partially folded proteins
Malene Ringkjøbing Jensen1, Martin Blackledge
1Protein Dynamics and Flexibility by NMR, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; CNRS; UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, France.
Abstract:
The presence of dipolar coupling waves within helical elements of proteins implies an effective tilt of the main axis of the helical element relative to the magnetic field. Here, we investigate the origin of dipolar waves observed in helical elements of partially folded proteins. We find that the dipolar waves result from an effective tilt of the helix relative to the alignment axis that is determined by the directionality of the unfolded chains projected from the helix caps. The amplitude and phase of the dipolar wave depend in a predictable way on helix length, providing direct insight into helix stability, nucleation, and fraying in partially folded proteins.
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