ArticleMethods in molecular biology (Clifton, N.J.)2026
Förster Resonance Energy Transfer as a Tool for Quantification of Protein-Lipid Selectivity.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
This chapter addresses the determination of protein-lipid selectivity, which is described as the preference of a protein for a specific type of lipid in its vicinity. Specifically, Förster resonance energy transfer (FRET) methodologies are used for quantification of this effect. FRET enables the determination of biasing in the distribution of the lipid under study around the protein, as compared to its bulk membrane distribution, with advantages over alternative established approaches, such as electron spin resonance spectroscopy. The experiment can be carried out in either steady-state or time-resolved conditions. Formalisms valid for both situations are described in detail. They apply to both transmembrane-spanning and lipid/water interface-bound proteins of any size.
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