Quantification of protein-lipid selectivity using FRET.
Membrane proteins exhibit different affinities for different lipid species, and protein-lipid selectivity regulates the membrane composition in close proximity to the protein, playing an important role in the formation of nanoscale membrane heterogeneities. The sensitivity of Förster resonance energy transfer (FRET) for distances of 10 A up to 100 A is particularly useful to retrieve information on the relative distribution of proteins and lipids in the range over which protein-lipid selectivity is expected to influence membrane composition. Several FRET-based methods applied to the quantification of protein-lipid selectivity are described herein, and different formalisms applied to the analysis of FRET data for particular geometries of donor-acceptor distribution are critically assessed.
Loura
Luís M S
LM
Faculdade de Farmácia, Universidade de Coimbra, Pólo das Ciências da Saúde, Azinhaga de Santa Comba, 3000-548 Coimbra, Portugal.
Prieto
Manuel
M
Fernandes
Fábio
F
D000818:Animals; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011485:Protein Binding; D013379:Substrate Specificity
D008563:Membrane Lipids; D008565:Membrane Proteins