期刊
CHEMPHYSCHEM
卷 18, 期 17, 页码 2318-2321出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cphc.201700666
关键词
complexes; distance measurements; EPR spectroscopy; metalloproteins; multimers
资金
- EPSRC
- Wellcome Trust [099149/Z/12/Z]
- Royal Society [RG140723]
- European Union [PCIG12-GA-2012-334496]
- Wellcome Trust [099149/Z/12/Z] Funding Source: Wellcome Trust
- EPSRC [1792319] Funding Source: UKRI
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 Cu-II 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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