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Monitoring complex formation by relaxation-induced pulse electron paramagnetic resonance distance measurements

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Author(s)

Angeliki Giannoulis, Maria Oranges, Bela E. Bode

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Abstract

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.
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Original languageEnglish
Pages (from-to)2318-2321
Number of pages5
JournalChemPhysChem
Volume18
Issue number17
Early online date1 Aug 2017
DOIs
StatePublished - 6 Sep 2017

    Research areas

  • Complexes, Distance measurements, EPR spectroscopy, Metalloproteins, Multimers

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