ReviewEuropean biophysics journal : EBJ2010
Electron spin resonance in membrane research: protein-lipid interactions from challenging beginnings to state of the art.
Review in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Development of an EPR-based methodology to study protein-lipid interaction.Biophysical chemistry · 2026Article
- Effects of Lipopolysaccharides fromMembranes · 2026Article
- Non-Linear Continuous Wave Electron Paramagnetic Resonance Spectroscopy for Investigation of Lipid-Protein Interactions in Membranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Electron Paramagnetic Resonance Spectroscopy of Spin-Labeled Lipids for Studying Lipid-Protein Interaction in Model and Biomembranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Miltefosine analogues with comparable antileishmanial activity and significantly reduced macrophage cytotoxicity.Memorias do Instituto Oswaldo Cruz · 2025Article
- Lipid and protein dynamics of stacked and cation-depletion induced unstacked thylakoid membranes.BBA advances · 2021Article
- Ion channels as lipid sensors: from structures to mechanisms.Nature chemical biology · 2020Review
- Bioinspired Nanoemulsions Stabilized by Phosphoethanolamine and Phosphoglycerol Lipids.Nanomaterials (Basel, Switzerland) · 2020Article
- Interaction of the Mechanosensitive Channel, MscS, with the Membrane Bilayer through Lipid Intercalation into Grooves and Pockets.Journal of molecular biology · 2019Article
- Direct Prediction of EPR Spectra from Lipid Bilayers: Understanding Structure and Dynamics in Biological Membranes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2018Article
- Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.Cellular and molecular life sciences : CMLS · 2018Review
- The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.The Journal of membrane biology · 2017Article
- Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Biochimica et biophysica acta · 2016Review
- Lipid Librations at the Interface with the Na,K-ATPase.Biophysical journal · 2015Article
- Peptide-Membrane Interactions by Spin-Labeling EPR.Methods in enzymology · 2015Article
- Depolarization Laplace transform analysis of exchangeable hyperpolarized ¹²⁹Xe for detecting ordering phases and cholesterol content of biomembrane models.Biophysical journal · 2014Article
- Lipid-protein interactions in plasma membranes of fiber cells isolated from the human eye lens.Experimental eye research · 2014Article
- How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains.Frontiers in physiology · 2013Article
- Nanodiscs as a new tool to examine lipid-protein interactions.Methods in molecular biology (Clifton, N.J.) · 2013Review
- Prediction of lipid-binding regions in cytoplasmic and extracellular loops of membrane proteins as exemplified by protein translocation membrane proteins.The Journal of membrane biology · 2013Article
Corrections and comments
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Authors and funding
1 author.
Funding
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Abstract
Conventional electron paramagnetic resonance (EPR) spectra of lipids that are spin-labelled close to the terminal methyl end of the acyl chains are able to resolve the lipids directly contacting the protein from those in the fluid bilayer regions of the membrane. This allows determination of both the stoichiometry of lipid-protein interaction (i.e., number of lipid sites at the protein perimeter) and the selectivity of the protein for different lipid species (i.e., association constants relative to the background lipid). Spin-label EPR data are summarised for 20 or more different transmembrane peptides and proteins, and 7 distinct species of lipids. Lineshape simulations of the two-component conventional spin-label EPR spectra allow estimation of the rate at which protein-associated lipids exchange with those in the bulk fluid regions of the membrane. For lipids that do not display a selectivity for the protein, the intrinsic off-rates for exchange are in the region of 10 MHz: less than 10x slower than the rates of diffusive exchange in fluid lipid membranes. Lipids with an affinity for the protein, relative to the background lipid, have off-rates for leaving the protein that are correspondingly slower. Non-linear EPR, which depends on saturation of the spectrum at high radiation intensities, is optimally sensitive to dynamics on the timescale of spin-lattice relaxation, i.e., the microsecond regime. Both progressive saturation and saturation transfer EPR experiments provide definitive evidence that lipids at the protein interface are exchanging on this timescale. The sensitivity of non-linear EPR to low frequencies of spin exchange also allows the location of spin-labelled membrane protein residues relative to those of spin-labelled lipids, in double-labelling experiments.
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