Journal ArticleDOI
High hydrostatic pressure equipment for neutron scattering studies of samples in solutions
Judith Peters,Marcus Trapp,Darren J. Hughes,Steven Rowe,Bruno Demé,Jean-Luc Laborier,Claude Payre,Jean-Paul Gonzales,Simon Baudoin,Nadir Belkhier,Eddy Lelièvre-Berna +10 more
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TLDR
In this paper, the design of new high pressure equipment for structural and dynamical studies on samples in solution is described, and two sample cells for applying pressures up to 150 and 700 MPa (i.e. 1.5 and 7 MPa), respectively, are mounted on special sticks and inserted into the calorimeter of a cryostat to regulate the temperature.Abstract:
The design of new high pressure equipment for structural and dynamical studies on samples in solution is described. We present two sample cells for applying pressures up to 150 and 700 MPa (i.e. 1.5 and 7 kbar), respectively. These cells are mounted on special sticks and inserted into the calorimeter of a cryostat to regulate the temperature. Different parts of the equipment – the pressure controller, the sticks and the cells – are described. In addition, radiography tests which were performed with neutrons in situ at the Institut Laue Langevin to verify the tightness of the cells and the hydrostatic transmission of the pressure to the sample are presented. First results on model lipids are in agreement with former results by R. Winter et al. [Towards an understanding of the temperature/pressure configurational and free-energy landscape of biomolecules, J. Non-Equilib. Thermodyn. 32 (2007), pp. 41–97].read more
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High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes.
Nicolas Martinez,Grégoire Michoud,Anaïs Cario,Jacques Ollivier,Bruno Franzetti,Mohamed Jebbar,Philippe Oger,Philippe Oger,Judith Peters +8 more
TL;DR: In this article, water and protein dynamics on a nanometer scale were measured by quasi-elastic neutron scattering in the piezophile archaeon Thermococcus barophilus and the closely related pressure-sensitive T. kodakarensis.
Journal ArticleDOI
Influence of pressure and crowding on the sub-nanosecond dynamics of globular proteins.
TL;DR: With increasing pressure, a reduction in the dynamics of H atoms of folded lysozyme is found, suggesting a loss in protein mobility that follows a change in the local energy landscape upon the increase in packing density.
Journal ArticleDOI
Pressure-induced molten globule state of human acetylcholinesterase: structural and dynamical changes monitored by neutron scattering
Jérémie Marion,Marie Trovaslet,Nicolas Martinez,Patrick Masson,Patrick Masson,Ralf Schweins,Florian Nachon,Marcus Trapp,Marcus Trapp,Judith Peters +9 more
TL;DR: At atmospheric pressure, the SANS results obtained on D11 at ILL give a radius of gyration close to that calculated for a mixture of monomers, dimers and tetramers of the enzyme, suggesting a good agreement between hAChE crystal structure and its conformation in solution.
Journal ArticleDOI
High hydrostatic pressure effects investigated by neutron scattering on lipid multilamellar vesicles
Marcus Trapp,Marcus Trapp,Jérémie Marion,Moeava Tehei,Bruno Demé,Thomas Gutberlet,Judith Peters +6 more
TL;DR: Backscattering spectroscopy reveals that the mean square displacements in the liquid phase are about 10% smaller at 300 bar and about 20% bigger at 600 bar compared to atmospheric pressure, whereas in the gel phase below the main phase transition the meansquare displacements show a smaller difference in the dynamics of the three pressure values within the studied pressure range.
Journal ArticleDOI
Influence of cosolvents, self-crowding, temperature and pressure on the sub-nanosecond dynamics and folding stability of lysozyme
TL;DR: A stabilization of the protein in the presence of the compatible osmolyte TMAO and a destabilizing effect upon self-crowding at very high protein concentration are observed, which is attributable to transient destabilizing intermolecular interactions.
References
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Journal ArticleDOI
Protein dynamics studied by neutron scattering.
TL;DR: This review of protein dynamics studied by neutron scattering focuses on data collected in the last 10 years and concerns the strong dependence of internal dynamics on the macromolecular environment.
Journal ArticleDOI
Protein dynamics: comparison of simulations with inelastic neutron scattering experiments.
TL;DR: To deepen the understanding of the principles determining the folding and functioning of globular proteins the determination of their three-dimensional structures must be supplemented with the characterization of their internal motions.
Journal ArticleDOI
Towards an Understanding of the Temperature/ Pressure Configurational and Free-Energy Landscape of Biomolecules
TL;DR: In this article, the effect of various types of cosolvents on the temperature and pressure-dependent structure and stability of proteins was studied, and pressure was also introduced as a kinetic variable.
Journal ArticleDOI
Hydrostatic limits of Fluorinert liquids used for neutron and transport studies at high pressure
V A Sidorov,Ravil A. Sadykov +1 more
TL;DR: In this article, the authors determined the hydrostatic limits at room temperature for a number of Fluorinert liquids: FC70, FC75, FC77, FC84, FC87 and their mixtures.