BBA reportDistinct states of lipid mobility in bovine rod outer segment membranes Resolution of spin label results
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Cited by (50)
Non-covalent binding of membrane lipids to membrane proteins
2014, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :As noted above, this is likely the result of rapid decay of the solid echo in those experiments. Another factor is the ability of an acyl chain to move off and back on the protein when the lipid headgroup is bound to the protein [89]. Finally other techniques also suggest the presence of two lipid components in membranes containing the calcium pump.
Protein modulation of lipids, and vice-versa, in membranes
2008, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Correspondingly, experiments with spin-labelled lipids do not detect a significant change in the number of first-shell lipids on mild bleaching of rhodopsin to the meta-II state [133]. Because rhodopsin displays very little selectivity between different lipid headgroups [4,31,33,133], the influence of lipid–protein interactions should be felt primarily in the lipid chain regions. With a change in excess free energy density of ΔgLP(ch ≈ 2.2 × kBT per nm2 (see above) and a hydrophobic span for rhodopsin of 3.2 ± 0.2 nm [134], Eq. (9) then predicts a change in chemical potential on changing lipid composition of 4.4 ± 0.3 × kBT, for a conformational change with ΔrP ≈ 0.1 nm.
Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes
2007, Biophysical JournalCitation Excerpt :A change of this magnitude would involve the displacement, or incorporation, of effectively just one lipid in the first shell at the perimeter of the transmembrane protein. Correspondingly, experiments with spin-labeled lipids do not detect a significant change in the number of first-shell lipids on mild bleaching of rhodopsin to the meta-II state (97). Hong and Tamm (26), in a series of experiments with systematically varying lipid composition, have demonstrated reversible urea-induced unfolding of the β-barrel outer membrane protein OmpA in small unilamellar vesicles (SUVs of mean diameter 300 Å).
Effect of packing density on rhodopsin stability and function in polyunsaturated membranes
2005, Biophysical JournalCitation Excerpt :There are 22–24 phospholipid molecules located in the annular lipid layer surrounding rhodopsin (43,44). Those phospholipids have hindered motion due to direct interaction with rhodopsin (44–47). At rhodopsin/lipid ratios ranging from 1:422 to 1:40, ∼6% to 60% of the phospholipids are located in the annular layer.
The nature of the lipid-protein interface and the influence of protein structure on protein-lipid interactions
1993, New Comprehensive Biochemistry