Spins Afar─Long-Range Pulse Dipolar EPR Spectroscopy Uncovers Curvature in TRIM25's Coiled Coil.
- 1EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic Resonance, University of St.Andrews, North Haugh, St AndrewsKY16 9ST, 248 ScotlandUK.
- 2Clausius-Institute for Physical and Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53115Bonn, Germany.
- 3School of Life Sciences, University of Dundee, Medical Sciences Institute, Nethergate DundeeDD1 4HN, Scotland, UK.
Abstract
Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy (PDS) is a powerful method for determining nanometer distances in biomolecular systems. This methodology has been successfully used to validate structure hypotheses and to identify disorder. However, inherent distance limitations are under-explored. Many challenging biomolecular applications require long distance information, driving the need for a benchmarking study. We demonstrate distances up to 10.5 nm in TRIM25 reliably extracted from data obtained under standard sample conditions. By protein perdeuteration accurate distance measurements up to 17.3 nm were enabled. Enhancing sensitivity through optimization of the measurement and sample preparation conditions the achievable dipolar evolution time was extended to 150 μs. Thus, distances close to 20 nm should become experimentally accessible, highlighting the potential of advanced PDS methodologies for probing previously inaccessible long-range structural information in complex systems.
Related
- Peptide-Directed Ligand Design Enables Chemical Disruption of the Nrf2/MafG Coiled-Coil Transcription Factor Complex.
- Molecular Flexibility and Electrostatic Interactions Drive the Nanoscale Structure of Coiled-Coil GM130 Protein Condensates
- Patient-derived separation-of-function mutations reveal specific role for BRCA1 coiled coil domain in genome stability.
- Experimental Validation of Coiled-Coil Architecture and Folding Dynamics in the Golgin Bug1
- Systematic Interrogation Uncovers Targetable Translational Control Elements within the CFTR 5' UTR
BibTeX
@article{limbach2026spins,
title = {{Spins Afar─Long-Range Pulse Dipolar EPR Spectroscopy Uncovers Curvature in TRIM25's Coiled Coil.}},
author = {Yannik Limbach and Katrin Ackermann and Aisika Chakraborty and David G Norman and Bela E Bode},
journal = {The journal of physical chemistry letters},
year = {2026},
month = oct,
doi = {10.1021/acs.jpclett.6c02671},
url = {https://europepmc.org/article/MED/42918236},
note = {CC BY},
}
RIS
TY - JOUR
TI - Spins Afar─Long-Range Pulse Dipolar EPR Spectroscopy Uncovers Curvature in TRIM25's Coiled Coil.
AU - Yannik Limbach
AU - Katrin Ackermann
AU - Aisika Chakraborty
AU - David G Norman
AU - Bela E Bode
PY - 2026
DA - 2026/10/01
JO - The journal of physical chemistry letters
DO - 10.1021/acs.jpclett.6c02671
UR - https://europepmc.org/article/MED/42918236
AB - Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy (PDS) is a powerful method for determining nanometer distances in biomolecular systems. This methodology has been successfully used to validate structure hypotheses and to identify disorder. However, inherent distance limitations are under-explored. Many challenging biomolecular applications require long distance information, driving the need for a benchmarking study. We demonstrate distances up to 10.5 nm in TRIM25 reliably extracted from data obtained under standard sample conditions. By protein perdeuteration accurate distance measurements up to 17.3 nm were enabled. Enhancing sensitivity through optimization of the measurement and sample preparation conditions the achievable dipolar evolution time was extended to 150 μs. Thus, distances close to 20 nm should become experimentally accessible, highlighting the potential of advanced PDS methodologies for probing previously inaccessible long-range structural information in complex systems.
SN - 1948-7185
ER -