Lipid-protein interactions with the Na,K-ATPase.
Studies of lipid interactions with membranous Na,K-ATPase by using electron spin resonance spectroscopy in conjunction with spin-labelled lipids are reviewed. The lipid stoichiometry, selectivity and exchange dynamics at the lipid-protein interface can be determined, in addition to information on the configuration and rotational dynamics of the protein-associated lipid chains. These parameters, particularly the stoichiometry and selectivity, are related directly to the intramembranous structure of the Na,K-ATPase, and can be used to check the integrity of extensively trypsinised preparations.
Department of Biophysics, Institute of Physiology and Biophysics, University of Aarhus, Denmark. me@biophys.au.dk
Mikael
M
Esmann
Derek
D
Marsh
D002308:Cardiolipins / Q000737:chemistry / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D050356:Lipid Metabolism; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008956:Models, Chemical; D009994:Osmolar Concentration; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000378:metabolism*; D013113:Spin Labels; D014357:Trypsin / Q000378:metabolism
D002308:Cardiolipins; D008563:Membrane Lipids; D008565:Membrane Proteins; D013113:Spin Labels; D014357:Trypsin; D000254:Sodium-Potassium-Exchanging ATPase