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.
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February 2011
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Conference Article|
January 19 2011
Studying biomolecular complexes with pulsed electron–electron double resonance spectroscopy
Gunnar W. Reginsson;
Gunnar W. Reginsson
1Biomedical Sciences Research Complex, Centre of Magnetic Resonance, University of St Andrews, St Andrews KY16 9ST, UK
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Olav Schiemann
Olav Schiemann
1
1Biomedical Sciences Research Complex, Centre of Magnetic Resonance, University of St Andrews, St Andrews KY16 9ST, UK
1To whom correspondence should be addressed (email os11@st-andrews.ac.uk)
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Publisher: Portland Press Ltd
Received:
November 02 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (1): 128–139.
Article history
Received:
November 02 2010
Citation
Gunnar W. Reginsson, Olav Schiemann; Studying biomolecular complexes with pulsed electron–electron double resonance spectroscopy. Biochem Soc Trans 1 February 2011; 39 (1): 128–139. doi: https://doi.org/10.1042/BST0390128
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