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Sub-micromolar pulse dipolar EPR spectroscopy reveals increasing CuII-labelling of double-histidine motifs with lower temperature

Research output: Contribution to journalArticle

Abstract

Electron paramagnetic resonance (EPR) distance measurements are making increasingly important contributions to studies of biomolecules underpinning health and disease by providing highly accurate and precise geometric constraints. Combining double‐histidine motifs with CuII spin labels shows promise for further increasing the precision of distance measurements. It also appeals in proteins containing essential cysteines which can interfere with thiol‐specific labelling. However, the non‐covalent CuII coordination approach is vulnerable to low binding‐affinity. Here, dissociation constants (KD) are investigated directly from the cryoprotectant of relaxation induced dipolar modulation enhancement (RIDME) EPR distance experiments. The superb sensitivity of these experiments reveals low‐ to sub‐μM CuII KDs under EPR distance measurement conditions at cryogenic temperatures. We show the feasibility of exploiting the double histidine motif for EPR applications even at sub‐μM protein concentrations in orthogonally‐labelled Cu(II) ‐nitroxide systems using a commercial Q‐band EPR instrument.nd EPR instrument.
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Original languageEnglish
Pages (from-to)11807-11811
Number of pages6
JournalAngewandte Chemie
Volume131
Issue number34
Early online date18 Jul 2019
DOIs
Publication statusPublished - 19 Aug 2019

    Research areas

  • RIDME, Dissociation-constant, Double-histidine motif, Non-covalent interactions, EPR-spectroscopy

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