Related Experiment Video
Updated: Aug 17, 2026

Rapid Scan Electron Paramagnetic Resonance Opens New Avenues for Imaging Physiologically Important Parameters In Vivo
Published on: September 26, 2016
Pulsed EPR spectroscopy: biological applications
T Prisner1, M Rohrer, F MacMillan
1Institute for Physical and Theoretical Chemistry, J. W. Goethe-University Frankfurt, Marie-Curie-Strasse 11, Frankfurt am Main, D-60439 Germany. prisner@chemie.uni-frankfurt.de
Abstract:
Pulsed electron paramagnetic resonance (EPR) methods such as ESEEM, PELDOR, relaxation time measurements, transient EPR, high-field/high-frequency EPR, and pulsed ENDOR, have been used successfully to investigate the local structure and dynamics of paramagnetic centers in biological samples. These methods allow different contributions to the EPR spectra to be distinguished and can help unravel complicated EPR spectra consisting of overlapping resonance lines, as are often found in disordered protein samples. The basic principles, specific potentials, technical requirements, and limitations of these advanced EPR techniques will be reviewed together with recent applications to metal centers, organic radicals, and spin labels in proteins.
Related Concept Videos
Electron Paramagnetic Resonance (EPR) Spectroscopy: Organic Radicals
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences
Applications Of NMR In Biology
The...
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

