Patrick C. A. van der Wel- Solid-state NMR Group, Zernike Institute for Advanced Materials, University of Groningen, Groningen, Netherlands
A Correction on
Dihedral angle measurements for structure determination by biomolecular solid-state NMR spectroscopy
by van der Wel PCA (2021). Front. Mol. Biosci. 8:791090. doi: 10.3389/fmolb.2021.791090
There was a mistake in the caption of Figure 6 as published. The caption erroneously stated “(C,D) NCCH-type measurements of the φ backbone angle based on the same design principle (Ladizhansky et al., 2002)”. This text should have been referring to the ψ backbone angle. The corrected caption of Figure 6 appears below.
“FIGURE 6 Transfer-based torsion angle measurements of backbone angle ψ. (A,B) NCCN pulse sequence implemented without 13C DQ generation, using rotor-synchronized 13C-13C transfer instead (Ladizhansky et al., 2003). Carbonyl (C′) polarization is created via a double CP scheme, followed by REDOR-based 13C-15N recoupling (time tCN). The residual 13C′ signal is transferred to neighboring 13Cα via a short RFDR block, after which the 13Cα-15N recoupling is done (also for tCN). Finally, the remaining 13C signal (as a function of tCN) is recorded in a series of 1D or 2D N(CO)CA spectra (F). (C,D) NCCH-type measurements of the ψ backbone angle based on the same design principle (Ladizhansky et al., 2002). Here, 13C-1H dipolar recoupling occurred during the LGCP period. Note that here the REDOR time (tCN) and LGCP time (tCH) are both incremented in parallel. Panels B and D illustrate the generic design of these experiments, with color-coding of the dipolar recoupling blocks. (E) Structure of α-spectrin SH3, with residues L8 and V9 in the first β-strand marked (Musacchio et al., 1992), prepared with UCSF ChimeraX (Pettersen et al., 2021). (F) 2D N(CO)CA spectrum for uniformly labeled α-spectrin SH3, showing peaks for 13Cαi-15Ni+1 correlations between residues i and i+1. Peaks for the Cα of residues L8 and V9 are indicated with red ovals. (G) Example N(CO)CA NCCN data curves for L8 and V9, along with matching values of the ψ angle. (F,G) are adapted from (Ladizhansky et al., 2003) with permission, copyright American Chemical Society 2003.”
The original article has been updated.
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Keywords: solid-state NMR, structural biology, amyloid, polyglutamine, protein structures
Citation: van der Wel PCA (2025) Correction: Dihedral angle measurements for structure determination by biomolecular solid-state NMR spectroscopy. Front. Mol. Biosci. 12:1716334. doi: 10.3389/fmolb.2025.1716334
Received: 30 September 2025; Accepted: 06 October 2025;
Published: 07 November 2025.
Edited and reviewed by:
Amir Goldbourt, Tel Aviv University, IsraelCopyright © 2025 van der Wel. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Patrick C. A. van der Wel, cC5jLmEudmFuLmRlci53ZWxAcnVnLm5s