Electron Paramagnetic Resonance Spectroscopy in Biomolecular Studies
Summary
Electron Paramagnetic Resonance (EPR) spectroscopy is a powerful technique for probing unpaired electrons in biological macromolecules, offering unique insights into structure, dynamics and interactions. By detecting transitions between electron spin states under a magnetic field, EPR reveals local environments of paramagnetic centres or artificial spin labels introduced into proteins, nucleic acids and lipid assemblies. Pulsed variants such as Double Electron–Electron Resonance (DEER or PELDOR) measure nanometre‐scale distances between spin pairs, enabling characterisation of conformational ensembles and their modulation by ligands or environmental factors. Advances in instrumentation, labelling chemistry and data‐analysis algorithms have extended EPR applications from frozen solutions to living cells and operando conditions. This breadth has established EPR as a complementary tool to X-ray crystallography, cryo-electron microscopy and NMR spectroscopy, particularly for systems that are dynamic, heterogeneous or refractory to traditional structural methods. Recent developments underline the global significance of EPR in elucidating membrane protein mechanisms, enzyme conformational cycles and nucleic‐acid architectures, with practical implications for drug design, synthetic biology and materials science.
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Electron Paramagnetic Resonance Spectroscopy in Biomolecular Studies publication trend
The graph below shows the total number of articles in electron paramagnetic resonance spectroscopy in biomolecular studies across all publications each year (not limited to Nature Index journals).
Technical terms
Electron Paramagnetic Resonance (EPR): Spectroscopic method for detecting unpaired electrons by monitoring transitions between spin states in a magnetic field.
Double Electron–Electron Resonance (DEER/PELDOR): Pulsed EPR technique that measures dipolar interactions between two spin labels to derive distance distributions at the nanometre scale.
Spin Label: A stable radical moiety covalently or non‐covalently attached to a biomolecule to introduce an unpaired electron for EPR detection.
Nanodisc: A disc‐shaped lipid bilayer bounded by scaffold proteins, used to encapsulate membrane proteins in a native‐like environment for biophysical studies.
References
- Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in E. coli Cells. Angewandte Chemie International Edition (2023).
- Compact Electron Paramagnetic Resonance on a Chip Spectrometer Using a Single Sided Permanent Magnet. ACS Sensors (2024).
- In-Cell DEER Spectroscopy of Nanodisc-Delivered Membrane Proteins in Living Cell Membranes. JACS Au (2024).
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