Titlebook: Lipid-Protein Interactions; Methods and Protocol J?rg H. Kleinschmidt Book 2019Latest edition Springer Science+Business Media, LLC, part of

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,Quartz Crystal Microbalances as Tools for Probing Protein–Membrane Interactions,mation on a wealth of substrates and lipid compositions. SLBs provide a widely accepted and versatile model system which mimics the natural cell membrane separating the extracellular and intracellular fluids of the living cell. The quartz crystal microbalance with dissipation monitoring (QCM-D) has

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,Differential Scanning Calorimetry of Protein–Lipid Interactions,ced transitions. Since these properties might be affected by ligand binding, DSC is particularly useful for the characterization of protein interactions with biomimetic membranes. The advantages of this technique over other methods consist in the direct measurement of intrinsic thermal properties of

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Imaging and Force Spectroscopy of Single Transmembrane Proteins with the Atomic Force Microscope,er (nm) to millimeter (mm). The high temporal (millisecond) and spatial (nanometer) resolutions of the AFM are suited for studying many biological processes in their native conditions. The AFM cantilever—aptly termed as a “l(fā)ab on a tip”—can be used as an imaging tool as well as a handle to manipulat

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Kinetics of Insertion and Folding of Outer Membrane Proteins by Gel Electrophoresis,steps and involved intermediates or for the determination of activation energies. For many .-barrel transmembrane proteins (.-TMPs) it has been shown that the folded, functional form can be separated from the unfolded form by a simple electrophoretic mobility assay. The only requirements for a separ

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,Protein Microarrays and Liposome: A Method for Studying Lipid–Protein Interactions,nd powerful methods to identify lipid–protein interactions is using protein microarrays and liposomes. Liposomes are spherical vesicles that are surrounded by phospholipid bilayers in which the lipid of interest can be incorporated. Thus, liposomes can be used to detect lipid–protein interactions an

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