D
Daniel Lévy
Researcher at University of Paris
Publications - 58
Citations - 3260
Daniel Lévy is an academic researcher from University of Paris. The author has contributed to research in topics: Membrane protein & Lipid bilayer. The author has an hindex of 29, co-authored 58 publications receiving 2966 citations. Previous affiliations of Daniel Lévy include French Alternative Energies and Atomic Energy Commission & Pierre-and-Marie-Curie University.
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Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins.
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Bio-Beads: An Efficient Strategy for Two-Dimensional Crystallization of Membrane Proteins
Jean-Louis Rigaud,Gervaise Mosser,Jean-Jacques Lacapère,Anders Olofsson,Daniel Lévy,Jean-Luc Ranck,Jean-Luc Ranck +6 more
TL;DR: This work establishes the potential of Bio-Beads as a simple alternative to conventional dialysis for removing detergent and for obtaining 2D crystals of integral membrane proteins useful for structure analysis by electron crystallography.
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Detergent removal by non-polar polystyrene beads
TL;DR: The potential of polystyrene beads as a simple alternative to other conventional detergent removing strategies such as dialysis, gel chromatography and dilution is established and the usefulness of this detergent removal strategy to produce quasi-ideal proteoliposomes is evaluated.
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Activity of Transmembrane Proteins Induces Magnification of Shape Fluctuations of Lipid Membranes
TL;DR: The first experimental evidence of the effect of the activity of transmembrane proteins on shape fluctuations of a lipid membrane is reported, which is larger when the bacteriorhodopsin pumps protons than when it is not activated.
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High-resolution AFM of membrane proteins directly incorporated at high density in planar lipid bilayer.
Pierre-Emmanuel Milhiet,Francesca Gubellini,Alexandre Berquand,Patrice Dosset,Jean-Louis Rigaud,Christian Le Grimellec,Daniel Lévy +6 more
TL;DR: This approach provides an alternative experimental platform to the classical methods of two-dimensional crystallization of membrane proteins for the structural analysis by AFM and the versatility and simplicity of the method are important intrinsic properties for the conception of biosensors and nanobiomaterials involving membrane proteins.