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327 results on '"Chenal, Alexandre"'

55. Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin

Author

Karst, Johanna C., Perez, Ana Cristina Sotomayor, Guijarro, J. Inaki, Raynal, Bertrand, Chenal, Alexandre, and Ladant, Daniel

Subjects
Adenylate cyclase -- Chemical properties, Adenylate cyclase -- Structure, Calmodulin -- Chemical properties, Catalysis -- Analysis, Hydrodynamics -- Analysis, Hydrofoil boats -- Hydrodynamics, Hydrofoil boats -- Analysis, Biological sciences, Chemistry
Abstract

The biophysical property of the isolated catalytic domain in solution with or without calmodulin was explored to characterize the molecular basis of AC activation mechanism by calmodulin. A model for the structural transition between the calmodulin-free and calmodulin-bound AC was proposed on the basis of findings on calmodulin which triggered only minor modifications of the protein secondary and tertiary structure but exhibited pronounced effect on the hydrodynamic properties of AC.

Published
2010

56. Large size citrate-reduced gold colloids appear as optimal SERS substrates for cationic peptides

Author

López-Tobar, Eduardo, Hernández, Belén, Chenal, Alexandre, Coïc, Y.M., Gómez Santos, J., Mejía-Ospino, E., García-Ramos, José Vicente, Ghomi, Mahmoud, Sánchez-Cortés, Santiago, Universidad Industrial de Santander (Colombia), Colciencias (Colombia), and Ministerio de Economía y Competitividad (España)

Subjects
Surface-enhance Raman spectroscopy plasmonic nanoparticles, UV-visible absorption, Citrate-reduced gold colloids, Z-potential, Somatostatin-14, Octreotide, Transmission electron microscopy
Abstract

8 pags., 5 figs., 2 tabs., Surface-enhanced Raman spectra of two cyclic cationic peptides with therapeutic interest, somatostatin-14 and its synthetic analog octreotide, were simultaneously analyzed as a function of concentration and colloidal size. It appeared that the large size (~95 nm) citrate-reduced gold nanoparticles are the most adequate substrates for providing an optimal Raman signal enhancement within the 10–10 m peptide concentration range. It could also be evidenced that these large size particles can give rise to such a remarkable result within the first month following their elaboration. In fact, the recorded Raman spectra after this period mainly originate from the molecular species in the coverage of gold particles and not from the adsorbed peptides. To bring clarification to the temporal evolution of gold colloids, a systematic analysis was performed during 3 months on different particle sizes in the 15–150 nm range. The data obtained by a combined use of different techniques (Ultraviolet-visible absorption, z-potential, transmission electron microscopy, and Raman scattering) are consistent with a permanent evolution of the colloidal coverage, assignable to the gradual transformation of citrate anions and their substitution by oxidized products. It can be concluded that only small and medium size nanoparticles (≤ 40 nm) are able to regenerate their initial features after the first month, while large size colloids are subjected to a continuous degradation of their plasmonic and electrostatic properties. Copyright © 2016 John Wiley & Sons, Ltd., Funded by Spanish Ministerio de Economía y Competitividad. Grant Number: FIS2014-52212-R COLCIENCIAS. Grant Number: 511, 2010 Vicerrectoria de Investigación y Extensión (VIE) of Universidad Industrial de Santander (UIS). Grant Number: 5197

Published
2016

57. Side chain resonances in static oriented proton-decoupled [super 15]N solid-state NMR spectra of membrane proteins

Author

Aisenbrey, Christopher, Prongidi-Fix, Lydia, Chenal, Alexandre, Gillet, Daniel, and Bechinger, Burkhard

Subjects
Membrane proteins -- Structure, Membrane proteins -- Chemical properties, Nitrogen -- Atomic properties, Nitrogen -- Chemical properties, Nuclear magnetic resonance spectroscopy -- Usage, Chemistry
Abstract

Proton-decoupled [super 15]N solid-state NMR spectra are used to analyze the structure, dynamics, and membrane topology of proteins uniformly labeled with [super 15]N. The results from experimental and simulated [super 15]N spectra of oriented purple membranes, diphtheria toxin T domain and Bcl-xL demonstrated the possiblility to differentiate between side chain and backbone resonances.

Published
2009

63. Calcium Tightly Regulates Disorder-To-Order Transitions Involved in the Secretion, Folding and Functions of the CyaA Toxin of Bordetella Pertussis, the Causative Agent of Whooping Cough

Author

O’Brien, Darragh P., primary, Cannella, Sara E., additional, Durand, Dominique, additional, Ntsogo Enguéné, Véronique Y., additional, Hernandez, Belen, additional, Ghomi, Mahmoud, additional, Subrini, Orso, additional, Hessel, Audrey, additional, Malosse, Christian, additional, Hourdel, Véronique, additional, Vachette, Patrice, additional, Chamot-Rooke, Julia, additional, Brier, Sébastien, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2017
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65. Large size citrate-reduced gold colloids appear as optimal SERS substrates for cationic peptides

Author

Universidad Industrial de Santander (Colombia), Colciencias (Colombia), Ministerio de Economía y Competitividad (España), López-Tobar, Eduardo, Hernández, Belén, Chenal, Alexandre, Coïc, Y.M., Gómez Santos, J., Mejía-Ospino, E., García-Ramos, José Vicente, Ghomi, Mahmoud, Sánchez-Cortés, Santiago, Universidad Industrial de Santander (Colombia), Colciencias (Colombia), Ministerio de Economía y Competitividad (España), López-Tobar, Eduardo, Hernández, Belén, Chenal, Alexandre, Coïc, Y.M., Gómez Santos, J., Mejía-Ospino, E., García-Ramos, José Vicente, Ghomi, Mahmoud, and Sánchez-Cortés, Santiago

Abstract

Surface-enhanced Raman spectra of two cyclic cationic peptides with therapeutic interest, somatostatin-14 and its synthetic analog octreotide, were simultaneously analyzed as a function of concentration and colloidal size. It appeared that the large size (~95 nm) citrate-reduced gold nanoparticles are the most adequate substrates for providing an optimal Raman signal enhancement within the 10–10 m peptide concentration range. It could also be evidenced that these large size particles can give rise to such a remarkable result within the first month following their elaboration. In fact, the recorded Raman spectra after this period mainly originate from the molecular species in the coverage of gold particles and not from the adsorbed peptides. To bring clarification to the temporal evolution of gold colloids, a systematic analysis was performed during 3 months on different particle sizes in the 15–150 nm range. The data obtained by a combined use of different techniques (Ultraviolet-visible absorption, z-potential, transmission electron microscopy, and Raman scattering) are consistent with a permanent evolution of the colloidal coverage, assignable to the gradual transformation of citrate anions and their substitution by oxidized products. It can be concluded that only small and medium size nanoparticles (≤ 40 nm) are able to regenerate their initial features after the first month, while large size colloids are subjected to a continuous degradation of their plasmonic and electrostatic properties. Copyright © 2016 John Wiley & Sons, Ltd.

Published
2016

66. Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studies

Author

Selwa, Edithe, Davi, Marilyne, Chenal, Alexandre, Sotomayor-Pérez, Ana-Cristina, Ladant, Daniel, Malliavin, Thérèse E., Cellule Pasteur UPMC, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Pasteur [Paris] (IP), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Biochimie des Interactions Macromoléculaires, Edithe Selwa was supported by an allocation doctorale from MENRT, which was distributed by Universit ́e Pierre et Marie Curie (Paris VI).Ana Cristina Sotomayor Pérez was supported by an Institut Pasteur PTR grant (PTR#374). This project was supported by the Institut Pasteur and the Centre Nationalde la Recherche Scientifique (CNRS UMR3528, Biologie Structurale et Agents Infec-tieux)., Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Pasteur [Paris], Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

Subjects
animal structures, calcium, allostery, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], respiratory system, Molecular Dynamics Simulation, Protein Structure, Secondary, Bordetella pertussis, molecular dynamics, respiratory tract diseases, Protein Structure, Tertiary, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Allosteric Regulation, Bacterial Proteins, Calmodulin, Multiprotein Complexes, Adenylate Cyclase Toxin, Humans, calmodulin affin-ity, adenylyl cyclase, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Protein Structure, Quaternary, Molecular Biophysics
Abstract

International audience; Adenylyl cyclase (AC) toxin is an essential toxin that allows Bordetella pertussis to invade eukaryotic cells, where it is activated after binding to calmodulin (CaM). Based on the crystal structure of the AC catalytic domain in complex with the C-terminal half of CaM (C-CaM), our previous molecular dynamics simulations (Selwa, E., Laine, E., and Malliavin, T. (2012) Differential role of calmodulin and calcium ions in the stabilization of the catalytic domain of adenyl cyclase CyaA from Bordetella pertussis. Proteins 80, 1028–1040) suggested that three residues (i.e. Arg(338), Asn(347), and Asp(360)) might be important for stabilizing the AC/CaM interaction. These residues belong to a loop-helix-loop motif at the C-terminal end of AC, which is located at the interface between CaM and the AC catalytic loop. In the present study, we conducted the in silico and in vitro characterization of three AC variants, where one (Asn(347); ACm1A), two (Arg(338) and Asp(360); ACm2A), or three residues (Arg(338), Asn(347), and Asp(360); ACm3A) were substituted with Ala. Biochemical studies showed that the affinities of ACm1A and ACm2A for CaM were not affected significantly, whereas that of ACm3A was reduced dramatically. To understand the effects of these modifications, molecular dynamics simulations were performed based on the modified proteins. The molecular dynamics trajectories recorded for the ACm3AC-CaM complex showed that the calcium-binding loops of C-CaM exhibited large fluctuations, which could be related to the weakened interaction between ACm3A and its activator. Overall, our results suggest that the loop-helix-loop motif at the C-terminal end of AC is crucial during CaM binding for stabilizing the AC catalytic loop in an active configuration.

Published
2014

74. Anchoring sites of fibrillogenic peptide hormone somatostatin-14 on plasmonic nanoparticles

Author

Ministerio de Ciencia e Innovación (España), López-Tobar, Eduardo, Hernández, Belén, Gómez, Johanna, Chenal, Alexandre, García-Ramos, José Vicente, Ghomi, Mahmoud, Sánchez-Cortés, Santiago, Ministerio de Ciencia e Innovación (España), López-Tobar, Eduardo, Hernández, Belén, Gómez, Johanna, Chenal, Alexandre, García-Ramos, José Vicente, Ghomi, Mahmoud, and Sánchez-Cortés, Santiago

Abstract

© 2015 American Chemical Society. Despite numerous investigations devoted to the control of peptide and protein self-assemblies using nanostructured materials, the molecular details of the peptide-material interaction sites remain still under debate. Here, we suggest a solution by using jointly the middle- and low wavenumber regions of surface-enhanced Raman spectra. To achieve our goal, adequately prepared gold and silver colloids, of which the nanofabrication was controlled by means of zeta potential and extinction spectra, were used to enhance the Raman signal arising from a natural fibrillogenic peptide hormone, somatostatin-14, at very low (10-6-to-10-8 M) concentrations. Transmission electron microscopy has revealed that the interacting partners are involved in a mutual aggregation process. In fact, while the presence of plasmonic colloids facilitates the aggregation of the peptide, leading to the formation of the so-called >corona> around nanoparticles, we could observe the appearance of relatively large size peptide-nanoparticle agglomerates in solution. However, the comparison between the data obtained from gold and silver nanoparticles is consistent with the fact that the nature of metal surface, as well as its ionic coverage, considerably affect the peptide binding and subsequent aggregation process. Furthermore, this work led us to conclude that the adsorption of somatostatin-14 on silver nanoparticles is rendered possible through an ionic pair interaction, whereas its anchoring on gold nanoparticles occurs by a direct binding, in which the metal atom and the nitrogen of the unique peptide tryptophan residue are involved.

Published
2015

75. Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion

Author

O’Brien, Darragh P., primary, Hernandez, Belen, additional, Durand, Dominique, additional, Hourdel, Véronique, additional, Sotomayor-Pérez, Ana-Cristina, additional, Vachette, Patrice, additional, Ghomi, Mahmoud, additional, Chamot-Rooke, Julia, additional, Ladant, Daniel, additional, Brier, Sébastien, additional, and Chenal, Alexandre, additional

Published
2015
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76. The catalytic domains ofClostridium sordelliilethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid

Author

Varela Chavez, Carolina, primary, Hoos, Sylviane, additional, Haustant, Georges Michel, additional, Chenal, Alexandre, additional, England, Patrick, additional, Blondel, Arnaud, additional, Pauillac, Serge, additional, Lacy, D. Borden, additional, and Popoff, Michel Robert, additional

Published
2015
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79. Deciphering Protein Membrane Interactions Involved in the Translocation Process of a Bacterial Toxin, the Adenylate Cyclase (CyaA) Toxin from B. Pertussis

Author

Subrini, Orso, primary, Karst, Johanna, additional, Sotomayor-Pérez, Ana-Cristina, additional, Hessel, Audrey, additional, Selwa, Edithe, additional, Sapay, Nicolas, additional, Veneziano, Rémi, additional, Pansieri, Jonathan, additional, Chopineau, Joel, additional, Ladant, Daniel, additional, and Chenal, Alexandre, additional

Published
2015
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81. RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion

Author

Chenal, Alexandre, Ladant, Daniel, Delepierre, Muriel, Inaki Guijarro, J., Raynal, Bertrand, Biochimie des Interactions Macromoléculaires, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Résonance Magnétique Nucléaire des Biomolécules, Biophysique des Macromolécules et de leurs Interactions, and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Bacterial Proteins, Amino Acid Motifs, Adenylate Cyclase Toxin, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Calcium, Bordetella pertussis, Protein Binding, Protein Structure, Tertiary
Abstract

International audience; The Repeat in Toxin (RTX) motif is a tandemly repeated calcium-binding nonapeptide sequence present in proteins that are secreted by the type I secretion system (T1SS) of Gram-negative bacteria. Here, we have characterized the structural and hydrodynamic properties of the RTX Repeat Domain (RD) of the CyaA toxin from Bordetella pertussis. This 701-amino acid long domain contains about 40 RTX motifs. We showed that, in the absence of calcium, RD was natively disordered, weakly stable, and highly hydrated. Calcium binding induced compaction and dehydration of RD, along with the formation of stable secondary and tertiary structures. The calcium-induced conformational switch between unfolded conformations of apo-RD and stable structures of holo-RD is likely to be a key property for the biological function of the CyaA toxin: in the low calcium environment of the bacterial cytosol, the intrinsically disordered character of the protein may facilitate its secretion through the secretion machinery. In the extracellular medium, calcium binding can then trigger the folding of the polypeptide into its functional state. The intrinsic disorder of RTX-containing proteins in the absence of calcium may thus be directly involved in the efficient secretion of proteins through T1SS.

Published
2008

82. Membrane Interaction of Botulinum Neurotoxin ATranslocation (T) DomainTHE BELT REGION IS A REGULATORY LOOP FOR MEMBRANE INTERACTION

Author

Galloux, Marie, Vitrac, Heidi, Montagner, Caroline, Raffestin, Stephanie, Popoff, Michel R., Chenal, Alexandre, Forge, Vincent, Gillet, Daniel, Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Service d'Ingénierie Moléculaire pour la Santé (ex SIMOPRO) (SIMoS), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Bactéries anaérobies et Toxines, Institut Pasteur [Paris] (IP), Biochimie des Interactions Macromoléculaires, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the Commissariat à l'Energie Atomique (Signalization and Membrane Transport Program of the Life Science Division), Institut Pasteur [Paris], and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

Subjects
LIGHT-CHAIN, IDENTIFICATION, Static Electricity, DIPHTHERIA-TOXIN, Membranes, Artificial, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Hydrogen-Ion Concentration, Recombinant Proteins, Protein Structure, Tertiary, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Protein Transport, FUSION, CHANNEL, [SDV.TOX]Life Sciences [q-bio]/Toxicology, BINDING, CLOSTRIDIAL NEUROTOXINS, PROTEIN-RECEPTOR, PORE FORMATION, Isoelectric Point, Botulinum Toxins, Type A, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Protein Structure, Quaternary, Protein Binding, TETANUS
Abstract

International audience; The translocation of the catalytic domain through the membrane of the endosome to the cell cytoplasm is a key step of intoxication by botulinum neurotoxin (BoNT). This step is mediated by the translocation (T) domain upon endosome acidification, although the mechanism of interaction of the T domain with the membrane is still poorly understood. Using physicochemical approaches and spectroscopic methods, we studied the interaction of the BoNT/A T domain with the membrane as a function of pH. We found that the interaction with membranes does not involve major secondary or tertiary structural changes, as reported for other toxins like diphtheria toxin. The T domain becomes insoluble around its pI value and then penetrates into the membrane. At that stage, the T domain becomes able to permeabilize lipid vesicles. This occurs for pH values lower than 5.5, in agreement with the pH encountered by the toxin within endosomes. Electrostatic interactions are also important for the process. The role of the so-called belt region was investigated with four variant proteins presenting different lengths of the N-extremity of the T domain. We observed that this part of the T domain, which contains numerous negatively charged residues, limits the protein-membrane interaction. Indeed, interaction with the membrane of the protein deleted of this extremity takes place for higher pH values than for the entire T domain. Overall, the data suggest that acidification eliminates repulsive electrostatic interactions between the T domain and the membrane, allowing its penetration into the membrane without triggering detectable structural changes.

Published
2008

83. Large size citrate-reduced gold colloids appear as optimal SERS substrates for cationic peptides.

Author

López‐Tobar, Eduardo, Hernández, Belén, Chenal, Alexandre, Coïc, Yves‐Marie, Gómez Santos, Johanna, Mejía‐Ospino, Enrique, Garcia‐Ramos, José Vicente, Ghomi, Mahmoud, and Sanchez‐Cortes, Santiago

Subjects
GOLD nanoparticles spectra, SERS spectroscopy, COLLOIDAL gold, SOMATOSTATIN, CYCLIC peptides synthesis, CITRATES, TRANSMISSION electron microscopy
Abstract

Surface-enhanced Raman spectra of two cyclic cationic peptides with therapeutic interest, somatostatin-14 and its synthetic analog octreotide, were simultaneously analyzed as a function of concentration and colloidal size. It appeared that the large size (~95 nm) citrate-reduced gold nanoparticles are the most adequate substrates for providing an optimal Raman signal enhancement within the 10−6-10−7 m peptide concentration range. It could also be evidenced that these large size particles can give rise to such a remarkable result within the first month following their elaboration. In fact, the recorded Raman spectra after this period mainly originate from the molecular species in the coverage of gold particles and not from the adsorbed peptides. To bring clarification to the temporal evolution of gold colloids, a systematic analysis was performed during 3 months on different particle sizes in the 15-150 nm range. The data obtained by a combined use of different techniques (Ultraviolet-visible absorption, z-potential, transmission electron microscopy, and Raman scattering) are consistent with a permanent evolution of the colloidal coverage, assignable to the gradual transformation of citrate anions and their substitution by oxidized products. It can be concluded that only small and medium size nanoparticles (≤ 40 nm) are able to regenerate their initial features after the first month, while large size colloids are subjected to a continuous degradation of their plasmonic and electrostatic properties. Copyright © 2016 John Wiley & Sons, Ltd. [ABSTRACT FROM AUTHOR]

Published
2017
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93. Amyloid Fibrils Formed by the Programmed Cell Death Regulator Bcl-xL

Author

Chenal, Alexandre, primary, Vendrely, Charlotte, additional, Vitrac, Heidi, additional, Karst, Johanna C., additional, Gonneaud, Alexis, additional, Blanchet, Clément E., additional, Pichard, Sylvain, additional, Garcia, Elisabeth, additional, Salin, Bénédicte, additional, Catty, Patrice, additional, Gillet, Daniel, additional, Hussy, Nicolas, additional, Marquette, Christel, additional, Almunia, Christine, additional, and Forge, Vincent, additional

Published
2012
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98. Corrigendum to “Deciphering Membrane Insertion of the Diphtheria Toxin T Domain by Specular Neutron Reflectometry and Solid-State NMR Spectroscopy” [J. Mol. Biol. (2009) 391, 872–883]

Author

Chenal, Alexandre, primary, Prongidi-Fix, Lydia, additional, Perier, Aurélie, additional, Aisenbrey, Christopher, additional, Vernier, Grégory, additional, Lambotte, Stephan, additional, Haertlein, Michael, additional, Dauvergne, Marie-Thérèse, additional, Fragneto, Giovanna, additional, Bechinger, Burkhard, additional, Gillet, Daniel, additional, Forge, Vincent, additional, and Ferrand, Michel, additional

Published
2009
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99. Deciphering Membrane Insertion of the Diphtheria Toxin T Domain by Specular Neutron Reflectometry and Solid-State NMR Spectroscopy

Author

Chenal, Alexandre, primary, Prongidi-Fix, Lydia, additional, Perier, Aurélie, additional, Aisenbrey, Christopher, additional, Vernier, Grégory, additional, Lambotte, Stephan, additional, Fragneto, Giovanna, additional, Bechinger, Burkhard, additional, Gillet, Daniel, additional, Forge, Vincent, additional, and Ferrand, Michel, additional

Published
2009
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