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Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels

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Tkach,  I.
Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society;

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Bennati,  M.
Research Group of Electron Paramagnetic Resonance, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Tkach, I., Diederichsen, U., & Bennati, M. (2021). Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels. European Biophysics Journal, 50(2), 143-157. doi:10.1007/s00249-021-01508-6.


Cite as: http://hdl.handle.net/21.11116/0000-0008-6E5A-9
Abstract
Electron paramagnetic resonance (EPR)-based pulsed dipolar spectroscopy measures the dipolar interaction between paramagnetic centers that are separated by distances in the range of about 1.5–10 nm. Its application to transmembrane (TM) peptides in combination with modern spin labelling techniques provides a valuable tool to study peptide-to-lipid interactions at a molecular level, which permits access to key parameters characterizing the structural adaptation of model peptides incorporated in natural membranes. In this mini-review, we summarize our approach for distance and orientation measurements in lipid environment using novel semi-rigid TOPP [4-(3,3,5,5-tetramethyl-2,6-dioxo-4-oxylpiperazin-1-yl)-L-phenylglycine] labels specifically designed for incorporation in TM peptides. TOPP labels can report single peak distance distributions with sub-angstrom resolution, thus offering new capabilities for a variety of TM peptide investigations, such as monitoring of various helix conformations or measuring of tilt angles in membranes.