Studying biomolecular complexes with pulsed electron-electron double resonance spectroscopy.
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.
Biomedical Sciences Research Complex, Centre of Magnetic Resonance, University of St Andrews, St Andrews KY16 9ST, UK.
Gunnar W
GW
Reginsson
Olav
O
Schiemann
D018360:Crystallography, X-Ray; D004247:DNA / Q000032:analysis; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D031541:Fluorescence Resonance Energy Transfer; D046911:Macromolecular Substances / Q000032:analysis*; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000032:analysis; D013113:Spin Labels
D046911:Macromolecular Substances; D011506:Proteins; D013113:Spin Labels; D004247:DNA