Pulsed EPR Methods to Study Biomolecular Interactions

Authors

  • Irina Ritsch Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093 Zurich, SCS-Metrohm Award for best oral presentation in Physical Chemistry;, Email: irina.ritsch@phys.chem.ethz.ch
  • Daniel Klose Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093 Zurich
  • Henrik Hintz Faculty of Chemistry and Center for Molecular Materials (CM2), Bielefeld University, Universitätsstrasse 25, D33615 Bielefeld
  • Adelheid Godt Faculty of Chemistry and Center for Molecular Materials (CM2), Bielefeld University, Universitätsstrasse 25, D33615 Bielefeld
  • Gunnar Jeschke Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093 Zurich
  • Maxim Yulikov Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093 Zurich

DOI:

https://doi.org/10.2533/chimia.2019.268

PMID:

30975255

Keywords:

Deer, Orthogonal spin labelling, Pulsed dipolar spectroscopy, Ridme, Site-directed spin labelling

Abstract

Orthogonal site-directed spin labelling in combination with pulsed EPR spectroscopy is a powerful approach to study biomolecular interactions on a molecular level. Following a surge in pulse EPR method development, it is now possible to access distance distributions in the nanometre range in systems of complex composition. In this article we briefly outline the necessary considerations for measurements of distance distributions in macromolecular systems labelled with two or more different types of paramagnetic centres. We illustrate the approach with two examples: an application of the Double Electron-Electron Resonance (DEER) method on a triple spin-labelled protein dimer labelled with nitroxide and Gd(III), and an optimisation study of the Relaxation Induced Dipolar Modulation Enhancement (RIDME) experiment for the orthogonal spin pair Cu(II)-nitroxide.

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Published

2019-04-24