Interactions of lipids and proteins: some general principles.
Methods to describe the binding of phospholipids to membrane proteins are described. It is shown that it is difficult to obtain estimates of the number of phospholipids bound to the surface of a membrane protein from ESR experiments in which plots of free to bound spin label (y) vs. molar ratio of lipid to protein are extrapolated to y = 0. The relative advantages and disadvantages of ESR and fluorescence methods for measuring relative binding constants of phospholipids to membrane proteins are discussed. The particular problems associated with comparing binding constants of molecules of very different sizes (e.g., fatty acids and cardiolipin) are described and equations are presented to account for these problems. The possible effects of membrane viscosity and thickness on activity of membrane proteins are discussed, but it is concluded that effects of phospholipid structure on activity can only be understood in terms of a reasonably complete kinetic model for the protein.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D011485:Protein Binding; D012519:Sarcoplasmic Reticulum / Q000378:metabolism
D008565:Membrane Proteins; D010743:Phospholipids; D000251:Adenosine Triphosphatases