Articles | Volume 2, issue 1
Research article
16 Apr 2021
Research article |  | 16 Apr 2021

The decay of the refocused Hahn echo in double electron–electron resonance (DEER) experiments

Thorsten Bahrenberg, Samuel M. Jahn, Akiva Feintuch, Stefan Stoll, and Daniella Goldfarb

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Cited articles

Bahrenberg, T., Yang, Y., Goldfarb, D., and Feintuch, A.: rDEER: A Modified DEER Sequence for Distance Measurements Using Shaped Pulses, Magnetochemistry, 5, 20,, 2019. 
Bahrenberg, T., Jahn, S. M., Feintuch, A., Stoll, S., and Goldfarb, D.: The decay of the refocused Hahn echo in DEER experiments, Raw data, Zenodo,, 2021. 
Borbat, P. P., Georgieva, E. R., and Freed, J. H.: Improved sensitivity for long-distance measurements in biomolecules: Five-pulse double electron-electron resonance, J. Phys. Chem. Lett., 4, 170–175,, 2013. 
Breitgoff, F. D., Soetbeer, J., Doll, A., Jeschke, G., and Polyhach, Y. O.: Artefact suppression in 5-pulse double electron electron resonance for distance distribution measurements, Phys. Chem. Chem. Phys., 19, 15766–15779,, 2017. 
Brown, I.: Electron spin-echo studies of relaxation processes in molecular solids, in: Time Domain Electron Spin Resonance, edited by: Kevan, L. and Schwartz, R. N., John Wiley & Sons, New York, 195–229, 1979. 
Short summary
Double electron–electron resonance (DEER) provides information on the structure of proteins by attaching two spin labels to the protein at a well-defined location and measuring the distance between them. The sensitivity of the method in terms of the amount of the protein that is needed for the experiment depends strongly on the relaxation properties of the spin label and the composition of the solvent. We show how to set up the experiment for best sensitivity when the solvent is water (H2O).