ArticleBiophysical journal2004
Quantification of Protein-Lipid Selectivity using FRET: Application to the M13 Major Coat Protein.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Förster Resonance Energy Transfer as a Tool for Quantification of Protein-Lipid Selectivity.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Lipid-Protein Interactions in Plasma Membrane Organization and Function.Annual review of biophysics · 2022Review
- Using hydrogen/deuterium exchange mass spectrometry to define the specific interactions of the phospholipase A2 superfamily with lipid substrates, inhibitors, and membranes.The Journal of biological chemistry · 2013Review
- FRET in Membrane Biophysics: An Overview.Frontiers in physiology · 2011Article
- Transmembrane peptides influence the affinity of sterols for phospholipid bilayers.Biophysical journal · 2010Article
- Quantification of protein-lipid selectivity using FRET.European biophysics journal : EBJ · 2010Review
- Membrane protein frustration: protein incorporation into hydrophobic mismatched binary lipid mixtures.Biophysical journal · 2009Article
- Role of helix 0 of the N-BAR domain in membrane curvature generation.Biophysical journal · 2008Article
- FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein.Biophysical journal · 2007Article
- Motional restrictions of membrane proteins: a site-directed spin labeling study.Biophysical journal · 2006Article
- FRET study of membrane proteins: simulation-based fitting for analysis of membrane protein embedment and association.Biophysical journal · 2006Article
- Non-uniform membrane probe distribution in resonance energy transfer: application to protein-lipid selectivity.Journal of fluorescence · 2006Article
- Lipid bilayer topology of the transmembrane alpha-helix of M13 Major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy.Biophysical journal · 2004Article
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Authors and funding
7 authors.
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Abstract
Quantification of lipid selectivity by membrane proteins has been previously addressed mainly from electron spin resonance studies. We present here a new methodology for quantification of protein-lipid selectivity based on fluorescence resonance energy transfer. A mutant of M13 major coat protein was labeled with 7-diethylamino-3((4'iodoacetyl)amino)phenyl-4-methylcoumarin to be used as the donor in energy transfer studies. Phospholipids labeled with N-(7-nitro-2-1,3-benzoxadiazol-4-yl) were selected as the acceptors. The dependence of protein-lipid selectivity on both hydrophobic mismatch and headgroup family was determined. M13 major coat protein exhibited larger selectivity toward phospholipids which allow for a better hydrophobic matching. Increased selectivity was also observed for anionic phospholipids and the relative association constants agreed with the ones already presented in the literature and obtained through electron spin resonance studies. This result led us to conclude that fluorescence resonance energy transfer is a promising methodology in protein-lipid selectivity studies.
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