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Eva Pebay-Peyroula
Researcher at University of Grenoble
Publications - 90
Citations - 7106
Eva Pebay-Peyroula is an academic researcher from University of Grenoble. The author has contributed to research in topics: Bacteriorhodopsin & Membrane protein. The author has an hindex of 39, co-authored 87 publications receiving 6722 citations. Previous affiliations of Eva Pebay-Peyroula include Centre national de la recherche scientifique & Aix-Marseille University.
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Journal ArticleDOI
Structure of Mitochondrial Adp/ATP Carrier in Complex with Carboxyatractyloside
Eva Pebay-Peyroula,Cécile Dahout-Gonzalez,Richard Kahn,Véronique Trézéguet,Guy J.-M. Lauquin,Gérard Brandolin +5 more
TL;DR: The bovine carrier structure, together with earlier biochemical results, suggests that transport substrates bind to the bottom of the cavity and that translocation results from a transient transition from a ‘pit’ to a ’channel’ conformation.
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X-ray Structure of Bacteriorhodopsin at 2.5 Angstroms from Microcrystals Grown in Lipidic Cubic Phases
Eva Pebay-Peyroula,Gabriele Rummel,Gabriele Rummel,Jurg P. Rosenbusch,Jurg P. Rosenbusch,Ehud M. Landau,Ehud M. Landau +6 more
TL;DR: Findings reveal the constituents of the proton translocation pathway in the ground state, including loop conformations and side chain residues.
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Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution
Hassan Belrhali,Peter Nollert,Antoine Royant,Christoph Menzel,Jurg P. Rosenbusch,Ehud M. Landau,Eva Pebay-Peyroula +6 more
TL;DR: The structure of protein, lipid and water molecules in the crystals represents the functional entity of bR in the purple membrane of the bacteria at atomic resolution.
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High Resolution X-Ray Structure of an Early Intermediate in the Bacteriorhodopsin Photocycle
Karl Edman,Peter Nollert,Peter Nollert,Antoine Royant,Antoine Royant,Hassan Belrhali,Eva Pebay-Peyroula,Janos Hajdu,Richard Neutze,Ehud M. Landau +9 more
TL;DR: The high-resolution X-ray structure of an early intermediate in the photocycle of bacteriorhodopsin is described, which is formed directly after photoexcitation.
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NADPH oxidase activator p67phox behaves in solution as a multidomain protein with semi-flexible linkers
Dominique Durand,Corinne Vivès,Corinne Vivès,Dominique Cannella,Dominique Cannella,Javier Pérez,Eva Pebay-Peyroula,Eva Pebay-Peyroula,Patrice Vachette,Patrice Vachette,Franck Fieschi,Franck Fieschi +11 more
TL;DR: The SAXS analysis of p67(phox) reveals that it behaves as a multidomain protein with semi-flexible linkers and suggests that the protein is not as extended as unstructured linkers could allow, thereby implying the existence of intra-molecular interactions within p67 (phox).