Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels
| Autor: | Igor Tkach, Ulf Diederichsen, Marina Bennati |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Spin label
Transmembrane peptide Materials science DEER Biophysics Review SDSL 010402 general chemistry 01 natural sciences law.invention Paramagnetism PDS PELDOR Pulsed ESR β-peptide law Spectroscopy Spin (physics) Electron paramagnetic resonance 010405 organic chemistry Resolution (electron density) Cell Membrane Electron Spin Resonance Spectroscopy General Medicine Dipolar spectroscopy α-TOPP 0104 chemical sciences Membrane Chemical physics Helix Spin Labels Peptides β-TOPP |
| Zdroj: | European Biophysics Journal |
| Popis: | 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. Graphical Abstract |
| Databáze: | OpenAIRE |
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