Monitoring complex formation by relaxation-induced pulse electron paramagnetic resonance distance measurements
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Biomolecular complexes are often multimers fueling the demand for methods that allow unraveling their composition and geometric arrangement. Pulse electron paramagnetic resonance (EPR) spectroscopy is increasingly applied for retrieving geometric information on the nanometer scale. The emerging RIDME (relaxation-induced dipolar modulation enhancement) technique offers improved sensitivity in distance experiments involving metal centers (e.g. on metalloproteins or proteins labelled with metal ions). Here, a mixture of a spin labelled ligand with increasing amounts of paramagnetic CuII ions allowed accurate quantification of ligand-metal binding in the model complex formed. The distance measurement was highly accurate and critical aspects for identifying multimerization could be identified. The potential to quantify binding in addition to the high-precision distance measurement will further increase the scope of EPR applications.
Giannoulis , A , Oranges , M & Bode , B E 2017 , ' Monitoring complex formation by relaxation-induced pulse electron paramagnetic resonance distance measurements ' ChemPhysChem , vol 18 , no. 17 , pp. 2318-2321 . DOI: 10.1002/cphc.201700666
Copyright 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Funding: EPSRC DTC and Wellcome (099149/Z/12/Z).
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