2015
DOI: 10.1039/c5ay00599j
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A review of traditional and emerging methods to characterize lipid–protein interactions in biological membranes

Abstract: Lipid–protein interactions are essential for modulating membrane protein structures and biological functions in the cell plasma membrane. In this review we describe the salient features of classical and emerging methodologies for studying protein–lipid interactions and their limitations.

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Cited by 27 publications
(29 citation statements)
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“…Mobility of protein receptors, particularly those with transmembrane domains, can be a challenge in these platforms if the water gap is insufficient for limiting interaction between the protein and the glass support. To overcome this challenge, various cushions, such as polyethylene glycol (PEG) [52], bovine serum albumin, dextran [33,57], or polyelectrolyte brushes [54], have been placed between the bilayer and the supporting surface to improve protein mobility [58].…”
Section: Biomimetic Platformsmentioning
confidence: 99%
“…Mobility of protein receptors, particularly those with transmembrane domains, can be a challenge in these platforms if the water gap is insufficient for limiting interaction between the protein and the glass support. To overcome this challenge, various cushions, such as polyethylene glycol (PEG) [52], bovine serum albumin, dextran [33,57], or polyelectrolyte brushes [54], have been placed between the bilayer and the supporting surface to improve protein mobility [58].…”
Section: Biomimetic Platformsmentioning
confidence: 99%
“…There are various methods to visualize membrane curvatures in situ or in reconstituted systems such as X-ray crystallography [48,49], nuclear magnetic resonance spectroscopy (NMR) [50,51], fluorescence microscopy [52,53], and electron microscopy (EM) [54,55]. Use of these techniques provides an opportunity for scientists to decipher vast amounts of information about the molecular machinery underlying the membrane shape transformations at high resolution.…”
Section: Introductionmentioning
confidence: 99%
“…Membrane proteins represent approximately 25% of the human proteome, and they constitute more than 60% of current drug targets, due to their accessibility to extracellular molecules and roles in disease. [1][2][3][4] Strategies for the study of membrane protein interactions, and indeed interactions between proteins and membranes, 5 are therefore increasingly important to further our understanding of biomolecular function, both in fundamental research and drug discovery applications. However, membrane proteins are particularly challenging to study because they have large hydrophobic surfaces that can lead to misfolding or aggregation in aqueous solutions, as well as the low yield, solubility and stability of sample preparations.…”
Section: Introductionmentioning
confidence: 99%