Studying biomolecular complexes with pulsed electron-electron double resonance spectroscopy

Gunnar W. Reginsson, Olav Schiemann*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)


The function of biomolecules is intrinsically linked to their structure and the complexes they form during function. Techniques for the determination of structures and dynamics of these nanometre assemblies are therefore important for an understanding on the molecular level. PELDOR (pulsed electron-electron double resonance) is a pulsed EPR method that can be used to reliably and precisely measure distances in the range 1.5-8 nm, to unravel orientations and to determine the number of monomers in complexes. In conjunction with site-directed spin labelling, it can be applied to biomolecules of all sizes in aqueous solutions or membranes. PELDOR is therefore complementary to the methods of X-ray crystallography, NMR and FRET (fluorescence resonance energy transfer) and is becoming a powerful method for structural determination of biomolecules. In the present review, the methods of PELDOR are discussed and examples where PELDOR has been used to obtain structural information on biomolecules are summarized.

Original languageEnglish
Pages (from-to)128-139
Number of pages12
JournalBiochemical Society Transactions
Issue number1
Publication statusPublished - Feb 2011

Other keywords

  • Biomolecular complex
  • Double electron-electron resonance (DEER)
  • Electron paramagnetic resonance (EPR)
  • Pulsed electron-electron double resonance (PELDOR)
  • Spin labelling


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