Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Burkhard Annighöfer"'
Autor:
Jérôme Schwindling, Burkhard Annighöfer, Nicolas Chauvin, Jean-Louis Meuriot, Borana Mom, Frédéric Ott, Nadia Sellami, Loïc Thulliez
Publikováno v:
Journal of Neutron Research. 24:289-298
Following tests of low power bulk Beryllium targets in 2016–2020, a high power target was designed, built and tested at the High Intensity Proton Injector (IPHI) at CEA Paris–Saclay. The design of the target and the results of the tests will be d
Autor:
Simeon Minić, Burkhard Annighöfer, Arnaud Hélary, Laïla Sago, David Cornu, Annie Brûlet, Sophie Combet
Publikováno v:
Biophys J
Biophysical Journal
Biophysical Journal, 2022, 121 (13), pp.2514-2525. ⟨10.1016/j.bpj.2022.06.003⟩
Biophysical Journal
Biophysical Journal, 2022, 121 (13), pp.2514-2525. ⟨10.1016/j.bpj.2022.06.003⟩
International audience; High pressure (HP) is a particularly powerful tool to study protein folding/unfolding, revealing subtle structural rearrangements. Bovine β-lactoglobulin (BLG), a protein of interest in food science, exhibits a strong propens
Autor:
Burkhard Annighöfer, Camille Loupiac, Simeon Minić, Gaston Hui Bon Hoa, Sophie Combet, Annie Brûlet, Djemel Hamdane, Arnaud Hélary
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2020, 119 (11), pp.2262-2274. ⟨10.1016/j.bpj.2020.10.019⟩
Biophysical Journal, Biophysical Society, 2020, 119, pp.2262-2274. ⟨10.1016/j.bpj.2020.10.019⟩
Biophysical Journal, 2020, 119, pp.2262-2274. ⟨10.1016/j.bpj.2020.10.019⟩
Biophys J
Biophysical Journal, Biophysical Society, 2020, 119 (11), pp.2262-2274. ⟨10.1016/j.bpj.2020.10.019⟩
Biophysical Journal, Biophysical Society, 2020, 119, pp.2262-2274. ⟨10.1016/j.bpj.2020.10.019⟩
Biophysical Journal, 2020, 119, pp.2262-2274. ⟨10.1016/j.bpj.2020.10.019⟩
Biophys J
To probe intermediate states during unfolding and oligomerization of proteins remains a major challenge. High pressure (HP) is a powerful tool for studying these problems, revealing subtle structural changes in proteins not accessible by other means
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9f5cf8f3be93d97d617f895273eb2d8
https://hal-agrosup-dijon.archives-ouvertes.fr/hal-03047967
https://hal-agrosup-dijon.archives-ouvertes.fr/hal-03047967
Autor:
Annalisa Polidori, Mathieu Salanne, Anita Zeidler, Burkhard Annighöfer, Stefan Klotz, Ruth F. Rowlands, Henry E. Fischer, Philip S. Salmon
Publikováno v:
Polidori, A, Rowlands, R, Zeidler, A, Salanne, M, Fischer, H, Annighoefer, B, Klotz, S & Salmon, P 2021, ' Structure and dynamics of aqueous NaCl solutions at high temperatures and pressures ', Journal of Chemical Physics, vol. 155, no. 19, 194506 . https://doi.org/10.1063/5.0067166
The structure of a concentrated solution of NaCl in D2O was investigated by in situ high-pressure neutron diffraction with chlorine isotope substitution to give site-specific information on the coordination environment of the chloride ion. A broad ra
Publikováno v:
Annighoefer, B, Polidori, A, Zeidler, A, Fischer, H & Salmon, P 2017, ' High-pressure neutron diffraction apparatus for investigating the structure of liquids under hydrothermal conditions ', High Pressure Research, vol. 37, no. 4, pp. 529-544 . https://doi.org/10.1080/08957959.2017.1391953
A high-pressure setup is described for making neutron diffraction experiments on liquids under hydrothermal conditions. Designs are given for a modified Bridgman unsupported area seal, a fluid separator that keeps apart the liquid sample and pressuri
Autor:
L. Thulliez, Jérôme Schwindling, Frédéric Ott, Alain Menelle, A. Letourneau, Nadia Sellami, Burkhard Annighöfer, Nicolas Chauvin
Publikováno v:
EPJ Web of Conferences, Vol 239, p 17011 (2020)
Facilities providing bright thermal neutron beams are of primary importance for various research topics such as condensed matter experiments, neutron-imaging or medical applications. Currently these are mainly spallation sources and nuclear reactors.
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:326-340
We performed complementary inelastic neutron scattering (INS) experiments and molecular dynamics (MD) simulations to study the influence of pressure on the low-frequency vibrational modes of lysozyme in aqueous solution in the 1 atm–6 kbar range. I
Autor:
M. Plazanet, Jörg Pieper, Burkhard Annighöfer, M.-S. Appavou, Marie-Claire Bellissent-Funel, Gabriel Gibrat, A. Buchsteiner
Publikováno v:
Journal of Physics: Condensed Matter. 17:S3093-S3099
A new hydrostatic pressure cell designed for small-angle neutron scattering (SANS) and quasi-elastic neutron scattering (QENS) experiments on biomolecular solutions has been developed at the Laboratoire L?on Brillouin. SANS and QENS experiments on bo
Autor:
Burkhard Annighöfer, Roland P. May, Marie-Claire Bellissent-Funel, Constantin T. Craescu, Yves Blouquit, Liliane Assairi, Gaston Hui Bon Hoa, Gabriel Gibrat
Publikováno v:
Biochimica et biophysica acta. 1844(9)
Apo-calmodulin, a small soluble mainly α protein, is a calcium-dependent protein activator. Calcium binding affects the calmodulin conformation but also its stability. Calcium free form unfolds between 40 and 80 °C, whereas the calcium-saturated fo
Autor:
Daniela Russo, Burkhard Annighöfer, Camille Loupiac, Paolo Mariani, Francesco Spinozzi, Maria Grazia Ortore, Alessandro Paciaroni
Publikováno v:
Biochimica et biophysica acta. G, General subjects
1830 (2013): 4974–4980. doi:10.1016/j.bbagen.2013.06.040
info:cnr-pdr/source/autori:Russo, Daniela; Ortore, Maria Grazia; Spinozzi, Francesco; Mariani, Paolo; Loupiac, Camille; Annighofer, Burkhard; Paciaroni, Alessandro/titolo:The impact of high hydrostatic pressure on structure and dynamics of beta-lactoglobulin/doi:10.1016%2Fj.bbagen.2013.06.040/rivista:Biochimica et biophysica acta. G, General subjects (Print)/anno:2013/pagina_da:4974/pagina_a:4980/intervallo_pagine:4974–4980/volume:1830
Biochimica et Biophysica Acta (BBA)-General Subjects
Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2013, 1830 (10), pp.4974-4980. ⟨10.1016/j.bbagen.2013.06.040⟩
Biochimica et Biophysica Acta (BBA)-General Subjects, 2013, 1830 (10), pp.4974-4980. ⟨10.1016/j.bbagen.2013.06.040⟩
1830 (2013): 4974–4980. doi:10.1016/j.bbagen.2013.06.040
info:cnr-pdr/source/autori:Russo, Daniela; Ortore, Maria Grazia; Spinozzi, Francesco; Mariani, Paolo; Loupiac, Camille; Annighofer, Burkhard; Paciaroni, Alessandro/titolo:The impact of high hydrostatic pressure on structure and dynamics of beta-lactoglobulin/doi:10.1016%2Fj.bbagen.2013.06.040/rivista:Biochimica et biophysica acta. G, General subjects (Print)/anno:2013/pagina_da:4974/pagina_a:4980/intervallo_pagine:4974–4980/volume:1830
Biochimica et Biophysica Acta (BBA)-General Subjects
Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2013, 1830 (10), pp.4974-4980. ⟨10.1016/j.bbagen.2013.06.040⟩
Biochimica et Biophysica Acta (BBA)-General Subjects, 2013, 1830 (10), pp.4974-4980. ⟨10.1016/j.bbagen.2013.06.040⟩
Methods Combining small-angle X-ray and neutron scattering measurements with inelastic neutron scattering experiments, we investigated the impact of high hydrostatic pressure on the structure and dynamics of β-lactoglobulin (βLG) in aqueous solutio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a73108944dd5e0dc652bd5d46e4c0bb4
https://publications.cnr.it/doc/319478
https://publications.cnr.it/doc/319478