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Updated: Sep 10, 2025
Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
Published on: July 4, 2016
Specificity and reactivity of bromoacrylaldehyde spin labels
Dominik Gendreizig1, Christina Elsner1, Svetlana Kucher1
1Department of Physical Chemistry, Sciences II, University of Geneva, 30 Quai Ernest Ansermet, 1211 Geneva, Switzerland.
None:
Electron paramagnetic resonance (EPR) spectroscopy in combination with site-directed spin labelling provides information on structure and dynamics of biomolecules. Increasing the availability of spin labels with different properties is an elegant way to foster a more accurate analysis of the EPR data in relation to the biological problem investigated. In this study, we present a comparative investigation of labelling efficiency, surface accessibility, site specificity and width of the distance distributions obtained on two proteins with the nitroxide-based bromoacrylaldehyde spin label (BASL) versus the two commercial spin labels MTSL (methanethiosulfonate spin label) and MAP (maleimido proxyl). Based on the predicted distances from a rotamer library approach and on the experimental distance distributions, BASL is shown to provide generally narrower distance distributions compared to the other nitroxide labels. The exquisite surface specificity of BASL with respect to MAP could be successfully exploited to selectively label surface cysteines in proteins containing a high number of native cysteines. In addition, the distinct site-reactivity of BASL and MAP towards two surface-exposed cysteines was leveraged for orthogonal labelling strategies with nitroxide and gadolinium labels.
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