scholarly journals Spin-label ESR studies of lipid-protein interactions in thylakoid membranes

Biochemistry ◽  
1989 ◽  
Vol 28 (18) ◽  
pp. 7446-7452 ◽  
Author(s):  
Gang Li ◽  
Peter F. Knowles ◽  
Denis J. Murphy ◽  
Ikuo Nishida ◽  
Derek Marsh
Keyword(s):  
Protein Interactions ◽  
Spin Label ◽  
Thylakoid Membranes ◽  
Lipid Protein Interactions

scholarly journals ESR spin-label studies of lipid-protein interactions in membranes

1982 ◽  
Vol 37 (1) ◽  
pp. 265-274 ◽  
Author(s):  
D. Marsh ◽  
A. Watts ◽  
R.D. Pates ◽  
R. Uhl ◽  
P.F. Knowles ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Spin Label ◽  
Lipid Protein Interactions

Spin-label studies of lipid-protein interactions with reconstituted band 3, the human erythrocyte chloride-bicarbonate exchanger

1998 ◽  
Vol 76 (5) ◽  
pp. 815-822 ◽  
Author(s):  
Andrew M Taylor ◽  
Anthony Watts
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Protein Interactions ◽  
Spin Label ◽  
Acyl Chain ◽  
Lateral Diffusion ◽  
Band 3 ◽  
Paramagnetic Resonance ◽  
A Value ◽  
Lipid Protein Interactions ◽  
Electron Paramagnetic

Lipid-protein interactions in reconstituted band 3 preparations were investigated by using spin-labeled lipids in conjunction with electron paramagnetic resonance (EPR) spectroscopy. Purified erythrocyte band 3 was reconstituted into egg phosphatidylcholine liposomes at high protein density with preservation predominantly of the dimeric state. Lipid-protein associations were revealed by the presence of a component in the EPR spectra that, when compared to spectra obtained from protein-free bilayers, indicated that lipid chain motions are restricted by interactions with the protein. From the fraction of the motionally restricted component obtained from the phosphatidylcholine spin-label, a value of 64 ± 14 annular lipids per band 3 dimer was obtained. This agrees with a value of 62 for the number of lipids that may be accommodated around the electron density map of a band 3 dimer. Selectivity of various spin-labeled lipids for the protein revealed that androstanol had a lower affinity for the band 3 interface, whereas a distinct preference was observed for the negatively charged lipids phosphatidylglycerol and stearic acid over phosphatidylcholine. This preference for negatively charged lipids could not be screened by 1-M salt, indicating that electrostatic lipid-protein interactions are not dominant. Estimates of annular lipid exchange rates from measured acyl chain segmental motions suggested that the rate of exchange between bilayer and boundary lipids was ~106 s-1, at least an order of magnitude slower than the rate of lipid lateral diffusion in protein-free bilayers.Key words: band 3, reconstitution, electron paramagnetic resonance, lipid-protein interactions.

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