Pulse EPR distance measurements to study multimers and multimerisation

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Abstract

Pulse dipolar electron paramagnetic resonance (PD-EPR) has become a powerful tool for structural biology determining distances on the nanometre scale. Recent advances in hardware, methodology, and data analysis have widened the scope to complex biological systems. PD-EPR can be applied to systems containing lowly populated conformers or displaying large intrinsic flexibility, making them all but intractable for cryo-electron microscopy and crystallography. Membrane protein applications are of particular interest due to the intrinsic difficulties for obtaining high-resolution structures of all relevant conformations. Many drug targets involved in critical cell functions are multimeric channels or transporters. Here, common approaches for introducing spin labels for PD-EPR cause the presence of more than two electron spins per multimeric complex. This requires careful experimental design to overcome detrimental multi-spin effects and to secure sufficient distance resolution in presence of multiple distances. In addition to obtaining mere distances, PD-EPR can also provide information on multimerisation degrees allowing to study binding equilibria and to determine dissociation constants.
Original languageEnglish
Pages (from-to)1513-1521
Number of pages9
JournalMolecular Physics
Volume116
Issue number12
Early online date5 Jan 2018
DOIs
Publication statusPublished - 2018

Keywords

  • Electron paramagnetic resonance
  • PELDOR
  • DEER
  • RIDME
  • Multi-spin

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