M. Gro?, G. Auerbach, and R. Et-jaenicke, The catalytic activities of monomeric enzymes show complex pressure dependence, FEBS Letters, vol.32, issue.2-3, pp.256-260, 1993.
DOI : 10.1146/annurev.bi.46.070177.001555

K. Henzler?wildman and D. Et-kern, Dynamic personalities of proteins, Nature, vol.124, issue.7172, pp.964-972, 2007.
DOI : 10.1038/nature06522

H. Ichimori, T. Hata, H. Matsuki, and S. Et-kaneshina, Barotropic phase transitions and pressure-induced interdigitation on bilayer membranes of phospholipids with varying acyl chain lengths, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1414, issue.1-2, pp.165-174, 1998.
DOI : 10.1016/S0005-2736(98)00165-5

K. Prasad, S. Shashidhar, R. Gaber, B. Et-chandrasekhar, and S. , Pressure studies on two hydrated phospholipids ??? 1,2-dimyristoyl-phosphatidylcholine and 1,2-dipalmitoyl-phosphatidylcholine, Chemistry and Physics of Lipids, vol.43, issue.3, pp.227-235, 1987.
DOI : 10.1016/0009-3084(87)90010-7

B. Lönnerdal and E. L. Et-lien, Nutritional and Physiologic Significance of ??-Lactalbumin in Infants, Nutrition Reviews, vol.61, issue.9, pp.295-305, 2003.
DOI : 10.1301/nr.2003.sept.295-305

C. Loupiac, M. Bonetti, S. Pin, and P. Et-calmettes, ??-lactoglobulin under high pressure studied by small-angle neutron scattering, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1764, issue.2, pp.211-216, 2006.
DOI : 10.1016/j.bbapap.2005.10.012

A. Macdonald, A dilatometric investigation of the effects of general anaesthetics, alcohols and hydrostatic pressure on the phase transition in smectic mesophases of dipalmitoyl phosphatidylcholine, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.507, issue.1, pp.26-37, 1978.
DOI : 10.1016/0005-2736(78)90371-1

J. Nagle and D. Et-wilkinson, Lecithin bilayers. Density measurement and molecular interactions, Biophysical Journal, vol.23, issue.2, pp.159-175, 1978.
DOI : 10.1016/S0006-3495(78)85441-1

M. G. Ortore, F. Spinozzi, F. Carsughi, P. Mariani, M. Bonetti et al., High pressure small-angle neutron scattering study of the aggregation state of ??-lactoglobulin in water and in water/ethylene-glycol solutions, Chemical Physics Letters, vol.418, issue.4-6, pp.342-346, 2006.
DOI : 10.1016/j.cplett.2005.11.019

M. G. Ortore, F. Spinozzi, P. Mariani, A. Paciaroni, L. R. Barbosa et al., Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution, Journal of The Royal Society Interface, vol.12, issue.1, pp.619-634, 2009.
DOI : 10.1016/S0301-4622(02)00325-3

N. Osaka, S. Takata, T. Suzuki, H. Endo, and M. Et-shibayama, Comparison of heat- and pressure-induced gelation of ??-lactoglobulin aqueous solutions studied by small-angle neutron and dynamic light scattering, Polymer, vol.49, issue.12, pp.2957-2963, 2008.
DOI : 10.1016/j.polymer.2008.04.055

A. Rahman, K. S. Singwi, and A. Et-sjölander, Theory of Slow Neutron Scattering by Liquids. I, Physical Review, vol.12, issue.3, pp.986-996, 1962.
DOI : 10.13182/NSE62-A26066

N. Rivalain, J. Roquain, and G. Et-demazeau, Development of high hydrostatic pressure in biosciences: Pressure effect on biological structures and potential applications in Biotechnologies, Biotechnology Advances, vol.28, issue.6, pp.659-672, 2010.
DOI : 10.1016/j.biotechadv.2010.04.001
URL : https://hal.archives-ouvertes.fr/hal-00530402

V. A. Sidorov and R. A. Sadykov, Hydrostatic limits of Fluorinert liquids used for neutron and transport studies at high pressure, Journal of Physics: Condensed Matter, vol.17, issue.40, pp.3005-3008, 2005.
DOI : 10.1088/0953-8984/17/40/002

G. N. Somero, Adaptations to High Hydrostatic Pressure, Annual Review of Physiology, vol.54, issue.1, pp.557-577, 1992.
DOI : 10.1146/annurev.ph.54.030192.003013

J. R. Trudell, D. G. Payan, J. H. Chin, and E. N. Et-cohen, The antagonistic effect of an inhalation anesthetic and high pressure on the phase diagram of mixed dipalmitoyl-dimyristoylphosphatidylcholine bilayers., Proceedings of the National Academy of Sciences, vol.72, issue.1, pp.210-213, 1975.
DOI : 10.1073/pnas.72.1.210

R. Winter and W. Et-dzwolak, Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins, Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences, vol.363, issue.1827, pp.537-563, 2005.
DOI : 10.1098/rsta.2004.1507

R. Winter and C. Et-jeworrek, Effect of pressure on membranes, Soft Matter, vol.254, issue.243, pp.3157-3173, 2009.
DOI : 10.1016/S0167-4838(01)00333-8

K. Wood, D. J. Tobias, B. Kessler, F. Gabel, D. Oesterhelt et al., The Low-Temperature Inflection Observed in Neutron Scattering Measurements of Proteins Is Due to Methyl Rotation: Direct Evidence Using Isotope Labeling and Molecular Dynamics Simulations, Journal of the American Chemical Society, vol.132, issue.14, pp.4990-4991, 2010.
DOI : 10.1021/ja910502g

J. Yang, A. K. Dunker, J. R. Powers, S. Clark, and B. G. Et-swanson, ??-Lactoglobulin Molten Globule Induced by High Pressure, Journal of Agricultural and Food Chemistry, vol.49, issue.7, pp.3236-3243, 2001.
DOI : 10.1021/jf001226o

G. Zaccai, J. L. Roumestand, A. E. Schlessman, and B. Garcia, DGA/SSA 08co501 and BioMedef 0 PDH-2-NRBC-3-C-301) Jérémie Marion was supported by a PhD scholarship from the French Ministry for Research and Technology Bernhard Frick (ILL) Moeava Tehei (IHMRI) and Lars Meinhold for fruitful discussions and their technical help. Finally, we thank Mathieu Lemé (ILL) and all members of the SANE group Nadir Belkhier and Eddy Lelièvre-Berna) for their help during the development of the high-pressure equipment. This work benefited from SasView software, originally developed by the DANSE project under NSF award DMR-0520547, We gratefully acknowledge Thomas Gutberlet (HZB), Bruno Demé (ILL), 2000.

M. Somkuti, H. Bublin, L. Breiteneder, and . Smeller, Binding, and Pressure???Temperature Phase Diagram of Cod Parvalbumin: Gad m 1, Biochemistry, vol.51, issue.30, pp.5903-5911, 2012.
DOI : 10.1021/bi300403h

L. Sussman, M. Harel, F. Frolow, C. Oefner, A. Goldman et al., Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein, Science, vol.343, issue.6260, pp.872-879, 1991.
DOI : 10.1038/343771a0

D. A. Darvesh, C. Hopkins, and . Geula, Neurobiology of butyrylcholinesterase, Nature Reviews Neuroscience, vol.59, issue.2, pp.131-138, 2003.
DOI : 10.1212/WNL.59.4.563

J. L. Silman and . Sussman, Acetylcholinesterase: How is structure related to function?, Chemico-Biological Interactions, vol.175, issue.1-3, pp.3-10, 2008.
DOI : 10.1016/j.cbi.2008.05.035

A. Clery-barraud, H. Ordentlich, A. Grosfeld, P. Shafferman, and . Masson, Pressure and heat inactivation of recombinant human acetylcholinesterase, European Journal of Biochemistry, vol.1429, issue.120, pp.4297-4307, 2002.
DOI : 10.1016/S0167-4838(98)00253-2

M. Kobashigawa, K. Sakurai, and . Nitta, Effect of hydrostatic pressure on unfolding of ??-lactalbumin: Volumetric equivalence of the molten globule and unfolded state, Protein Science, vol.12, issue.12, pp.2765-2772, 1999.
DOI : 10.1016/0005-2795(73)90327-9

X. Zhang, A. Peng, J. Jones, and . Jonas, NMR Study of the Cold, Heat, and Pressure Unfolding of Ribonuclease A, Biochemistry, vol.34, issue.27, pp.8631-8641, 1995.
DOI : 10.1021/bi00027a012

J. A. Vidugiris, J. L. Markley, and C. A. Royer, Evidence for a molten globule-like transition state in protein folding from determination of activation volumes, Biochemistry, vol.34, issue.15, pp.4909-4912, 1995.
DOI : 10.1021/bi00015a001

S. Doster, W. Cusack, and . Petry, Dynamical transition of myoglobin revealed by inelastic neutron scattering, Nature, vol.337, issue.6209, pp.754-756, 1989.
DOI : 10.1038/337754a0

G. Zaccai, How Soft Is a Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering, Science, vol.288, issue.5471, pp.1604-1607, 2000.
DOI : 10.1126/science.288.5471.1604

P. Sacquin-mora, V. Sebban, B. Derrien, R. Frick, C. Lavery et al., Probing the Flexibility of the Bacterial Reaction Center:?? The Wild-Type Protein Is More Rigid Than Two Site-Specific Mutants, Biochemistry, vol.46, issue.51, pp.14960-14968, 2007.
DOI : 10.1021/bi7004416

D. Gabel, U. Bicout, M. Lehnert, M. Tehei, G. Weik et al., Protein dynamics studied by neutron scattering, Quarterly Reviews of Biophysics, vol.35, issue.4, pp.327-367, 2002.
DOI : 10.1017/S0033583502003840

S. Appavou, G. Gibrat, M. Bellissent-funel, M. Plazanet, J. Pieper et al., The influence of a medium pressure on the structure and dynamics of a bovine pancreatic trypsin inhibitor protein, Journal of Physics: Condensed Matter, vol.17, issue.40, pp.3093-3099, 2005.
DOI : 10.1088/0953-8984/17/40/012

S. Appavou, S. Busch, W. Doster, A. Gaspar, and T. Unruh, The influence of 2??kbar pressure on the global and internal dynamics of human hemoglobin observed by quasielastic neutron scattering, European Biophysics Journal, vol.61, issue.278, pp.705-714, 2011.
DOI : 10.1103/PhysRevE.61.2730

M. Peters, M. Trovaslet, F. Trapp, F. Nachon, E. Hill et al., Activity and molecular dynamics relationship within the family of human cholinesterases, Physical Chemistry Chemical Physics, vol.450, issue.19, pp.6764-6770, 2012.
DOI : 10.1038/nature06522

J. Karnovsky and L. A. Roots, A "DIRECT-COLORING" THIOCHOLINE METHOD FOR CHOLINESTERASES, Journal of Histochemistry & Cytochemistry, vol.12, issue.3, pp.219-221, 1964.
DOI : 10.1177/12.3.219

V. Konarev, V. V. Volkov, A. V. Sokolova, M. H. Koch, and D. I. Svergun, : a Windows PC-based system for small-angle scattering data analysis, Journal of Applied Crystallography, vol.36, issue.5, pp.1277-1282, 2003.
DOI : 10.1107/S0021889803012779

A. K. Rahman, A. Singwi, and . Sjölander, Theory of Slow Neutron Scattering by Liquids. I, Physical Review, vol.12, issue.3, pp.986-996, 1962.
DOI : 10.13182/NSE62-A26066

H. Paalman and C. J. Pings, Numerical Evaluation of X???Ray Absorption Factors for Cylindrical Samples and Annular Sample Cells, Journal of Applied Physics, vol.33, issue.8, pp.2635-2639, 1962.
DOI : 10.1063/1.1699919

M. Bon, M. Huet, F. Lemonnier, J. Rieger, and . Massoulié, Molecular Forms of Electrophorus Acetylcholinesterase. Molecular Weight and Composition, European Journal of Biochemistry, vol.419, issue.2, pp.523-530, 1976.
DOI : 10.1042/bj0271824

H. Gekko and . Noguchi, Compressibility of globular proteins in water at 25.degree.C, The Journal of Physical Chemistry, vol.83, issue.21, pp.2706-2714, 1979.
DOI : 10.1021/j100484a006

I. Dvir, M. Silman, T. L. Harel, J. L. Rosenberry, and . Sussman, Acetylcholinesterase: From 3D structure to function, Chemico-Biological Interactions, vol.187, issue.1-3, pp.10-22, 2010.
DOI : 10.1016/j.cbi.2010.01.042
URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2894301/pdf

M. J. Cheung, F. Rudolph, M. S. Burshteyn, E. N. Cassidy, J. Gary et al., Structures of Human Acetylcholinesterase in Complex with Pharmacologically Important Ligands, Journal of Medicinal Chemistry, vol.55, issue.22, pp.10282-10286, 2012.
DOI : 10.1021/jm300871x

. Tanford, Physical Chemistry of Macromolecules, Journal of The Electrochemical Society, vol.109, issue.3, 1961.
DOI : 10.1149/1.2425390

M. Trapp, F. Trovaslet, M. M. Nachon, L. V. Koza, F. Eijck et al., Acetylcholinesterase and Its Huperzine A-Inhibited Counterpart, The Journal of Physical Chemistry B, vol.116, issue.51, pp.14744-14753, 2012.
DOI : 10.1021/jp304704h
URL : https://hal.archives-ouvertes.fr/hal-01131840

G. Ortore, F. Spinozzi, P. Mariani, A. Paciaroni, L. R. Barbosa et al., Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution, Journal of The Royal Society Interface, vol.12, issue.1, pp.619-634
DOI : 10.1016/S0301-4622(02)00325-3

R. Girard, M. Kahn, A. C. Mezouar, T. W. Dhaussy, J. E. Lin et al., The First Crystal Structure of a Macromolecular Assembly under High Pressure: CpMV at 330 MPa, Biophysical Journal, vol.88, issue.5, pp.3562-3571, 2005.
DOI : 10.1529/biophysj.104.058636

V. Fu, V. R. Kasinath, N. V. Moorman, V. J. Nucci, A. J. Hilser et al., Coupled Motion in Proteins Revealed by Pressure Perturbation, Journal of the American Chemical Society, vol.134, issue.20, pp.8543-8550, 2012.
DOI : 10.1021/ja3004655
URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3415598/pdf

D. Bicout, Diffusion incoh??rente des neutrons??: mod??les analytiques pour la dynamique interne des prot??ines, Journal de Physique IV (Proceedings), vol.130, pp.115-132, 2005.
DOI : 10.1051/jp4:2005130008
URL : http://jp4.journaldephysique.org/articles/jp4/pdf/2005/08/jp4130008.pdf

F. Varley and . Sears, NIST (1992) Neutron News, pp.29-37

M. Bée, Quasielastic neutron scattering, 1988.

E. Fanchon, E. Geissler, J. Hodeau, J. Regnard, and P. A. Timmins, Structure and Dynamics of Biomolecules, pp.161-180, 2000.

L. Van-hove, Correlations in Space and Time and Born Approximation Scattering in Systems of Interacting Particles, Physical Review, vol.80, issue.1, p.249, 1954.
DOI : 10.1103/PhysRev.80.141

L. Van-hove, A remark on the time-dependent pair distribution, Physica, vol.24, issue.1-5, p.404, 1958.
DOI : 10.1016/S0031-8914(58)95629-5

S. Lovesey, Theory of thermal neutron scattering from condensed matter, International Series of Monographs on Physics, vol.72, 1984.

W. Doster, S. Cusack, and W. Petry, Dynamical transition of myoglobin revealed by inelastic neutron scattering, Nature, vol.337, issue.6209, pp.754-756, 1989.
DOI : 10.1038/337754a0

R. Scherm and T. Springer, Proposal of a Multiple Chopper for the Investigation of Very Small Energy Transfert, IFF J ? o lilch, 1967.

M. M. Williams, Random Processes in Nuclear Reactors, IEEE Transactions on Nuclear Science, vol.22, issue.5, 1974.
DOI : 10.1109/TNS.1975.4328076

A. Heidemann and J. L. Buevoz, IN13 : A high energy resolution spectrometer for short wavelengths, 1977.

X. Falourd, F. Natali, J. Peters, and L. Foucat, Molecular mobility in Medicago truncatula seed during early stage of germination: Neutron scattering and NMR investigations, Chemical Physics, vol.428, pp.181-185, 2014.
DOI : 10.1016/j.chemphys.2013.10.014
URL : https://hal.archives-ouvertes.fr/hal-01161769

W. Knoll, J. Peters, P. Kursula, Y. Gerelli, and F. Natali, Influence of myelin proteins on the structure and dynamics of a model membrane with emphasis on the low temperature regime, The Journal of Chemical Physics, vol.7, issue.6, 2014.
DOI : 10.1074/jbc.M311504200
URL : https://hal.archives-ouvertes.fr/hal-01582610

M. Trapp, J. Marion, M. Tehei, B. Demé, T. Gutberlet et al., High hydrostatic pressure effects investigated by neutron scattering on lipid multilamellar vesicles, Physical Chemistry Chemical Physics, vol.14, issue.48, pp.20951-20956, 2013.
DOI : 10.1002/cbic.201300244
URL : https://hal.archives-ouvertes.fr/hal-01664626

A. Cupane, M. Fomina, I. Piazza, J. Peters, ?. Schir et al., Experimental Evidence for a Liquid-Liquid Crossover in Deeply Cooled Confined Water, Physical Review Letters, vol.113, issue.21, 2014.
DOI : 10.1063/1.2897826
URL : https://hal.archives-ouvertes.fr/hal-01131235

F. Migliardo, M. T. Caccamo, and S. Magazô, Thermal Properties Investigation on Systems of Biophysical Interest by EINS and Wavelet Analysis, J. Phys. Chem. Biophys, vol.3, issue.118, pp.2161-0398, 2013.

K. Amann-winkel, F. Löw, P. H. Handle, W. Knoll, J. Peters et al., Limits of metastability in amorphous ices: the neutron scattering Debye???Waller factor, Physical Chemistry Chemical Physics, vol.125, issue.47, pp.16386-16391, 2012.
DOI : 10.1063/1.2378921

M. Grimaldo, F. Roosen-runge, F. Zhang, T. Seydel, and F. Schreiber, Diffusion and Dynamics of ??-Globulin in Crowded Aqueous Solutions, The Journal of Physical Chemistry B, vol.118, issue.25, pp.7203-7209, 2014.
DOI : 10.1021/jp504135z

D. I. Svergun, Restoring Low Resolution Structure of Biological Macromolecules from Solution Scattering Using Simulated Annealing, Biophysical Journal, vol.76, issue.6, pp.2879-2886, 1999.
DOI : 10.1016/S0006-3495(99)77443-6

D. Description, eu/instruments-support/instruments- groups/instruments/d16/ [25] Description D11 https ://www.ill.eu/instruments-support/instruments- groups

D. I. Svergun and K. H. Nierhaus, Ribosome, Journal of Biological Chemistry, vol.13, issue.19, pp.14432-14439, 2000.
DOI : 10.1107/S0021889897001830

P. Oger and M. Jebbar, The many ways of coping with pressure, Research in Microbiology, vol.161, issue.10, pp.799-809, 2010.
DOI : 10.1016/j.resmic.2010.09.017
URL : https://hal.archives-ouvertes.fr/hal-00618586

V. V. Mozhaev, K. Heremans, J. Frank, P. Masson, and C. Balny, High pressure effects on protein structure and function, Proteins: Structure, Function, and Genetics, vol.68, issue.1, pp.81-91, 1996.
DOI : 10.1016/S0006-3495(95)80384-X

R. Jaenicke, Protein stability and molecular adaptation to extreme conditions, EJB Reviews, pp.291-304, 1991.
DOI : 10.1007/978-3-642-77200-9_22

G. Zaccai, How Soft Is a Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering, Science, vol.288, issue.5471, pp.1604-1607, 2000.
DOI : 10.1126/science.288.5471.1604

M. Trapp, J. Marion, M. Tehei, B. Demé, T. Gutberlet et al., High hydrostatic pressure effects investigated by neutron scattering on lipid multilamellar vesicles, Physical Chemistry Chemical Physics, vol.14, issue.48, pp.20951-20956, 2013.
DOI : 10.1002/cbic.201300244
URL : https://hal.archives-ouvertes.fr/hal-01664626

D. Bicout and J. Zaccai, Protein Flexibility from the Dynamical Transition:A Force Constant Analysis, Biophysical Journal, vol.80, issue.3, pp.1115-1123, 2001.
DOI : 10.1016/S0006-3495(01)76089-4

B. Aoun, Direct comparison of elastic incoherent neutron scattering experiments with molecular dynamics simulations of DMPC phase transitions, 48 and references therein, 2016.
DOI : 10.1021/jp2102868

M. Monkenbusch, D. Richter, and R. Biehl, Observation of Protein Domain Motions by Neutron Spectroscopy, ChemPhysChem, vol.14, issue.6, pp.1188-1194, 2010.
DOI : 10.1002/pol.1976.180140101

M. Bée, Application de la diffusion in??lastique aux syst??mes d??sordonn??s, Journal de Physique IV (Proceedings), vol.111, pp.259-296, 2003.
DOI : 10.1051/jp4:2002826

M. Tehei, Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering, EMBO reports, vol.5, issue.1, pp.66-70, 2004.
DOI : 10.1038/sj.embor.7400049

H. Frauenfelder, F. Parak, and R. D. Young, Conformational Substates in Proteins, Annual Review of Biophysics and Biophysical Chemistry, vol.17, issue.1, pp.569-572, 1988.
DOI : 10.1146/annurev.bb.17.060188.002315

F. Natali, J. Peters, D. Russo, S. Barbieri, C. Chiapponi et al., IN13 backscattering spectrometer at ILL : Looking for motions in biological macromolecules and organisms, Neutron News, vol.19, pp.14-18, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00370471

D. Richard, M. Ferrand, and G. J. Kearley, Analysis and visualisation of neutron-scattering data, Journal of Neutron Research, vol.4, issue.1, pp.33-39, 1996.
DOI : 10.1080/10238169608200065

A. Rahman, K. S. Singwi, and A. Sjölander, Theory of Slow Neutron Scattering by Liquids. I, Physical Review, vol.12, issue.3, pp.986-996, 1962.
DOI : 10.13182/NSE62-A26066

M. Trapp, T. Gutberlet, F. Juranyi, T. Unruh, B. Demé et al., Hydration dependent studies of highly aligned multilayer lipid membranes by neutron scattering, The Journal of Chemical Physics, vol.19, issue.16, pp.164505-164512, 2010.
DOI : 10.1006/jmbi.2000.3978

J. Peters, M. T. Giudici-orticoni, G. Zaccai, and M. Guiral, Dynamics measured by neutron scattering correlates with the organization of bioenergetics complexes in natural membranes from hyperthermophile and mesophile bacteria, The European Physical Journal E, vol.44, issue.7, p.78, 2013.
DOI : 10.1021/bi051131l
URL : https://hal.archives-ouvertes.fr/hal-01662563

J. Peters, J. Marion, F. Becher, M. Trapp, T. Gutberlet et al., Thermodynamics of lipid large unilamellar vesicles in presence of sterols at high hydrostatic pressure

T. Heimburg, Thermal Biophysics of Membranes, 2007.
DOI : 10.1002/9783527611591

R. L. Biltonen, A statistical-thermodynamic view of cooperative structural changes in phospholilid bilayer membranes : their potential role in biological function, J. Chem. Thermodyn, pp.22-23, 1990.

M. Fuxreiter and A. Warshel, Origin of the Catalytic Power of Acetylcholinesterase:?? Computer Simulation Studies, Journal of the American Chemical Society, vol.120, issue.1, pp.183-194, 1998.
DOI : 10.1021/ja972326m

Y. Zhang, J. Kua, and J. A. Mccammon, Influence of Structural Fluctuation on Enzyme Reaction Energy Barriers in Combined Quantum Mechanical/Molecular Mechanical Studies, The Journal of Physical Chemistry B, vol.107, issue.18, pp.4459-4463, 2003.
DOI : 10.1021/jp022525e

M. Ohgushi and A. Wada, ???Molten-globule state???: a compact form of globular proteins with mobile side-chains, FEBS Letters, vol.22, issue.1, pp.21-24, 1983.
DOI : 10.1002/bip.360220115

C. Clery-barraud, A. Ordentlich, H. Grosfeld, A. Shafferman, and P. Masson, Pressure and heat inactivation of recombinant human acetylcholinesterase, European Journal of Biochemistry, vol.1429, issue.120, pp.4297-4307, 2002.
DOI : 10.1016/S0167-4838(98)00253-2

J. Marion, M. Trovaslet, N. Martinez, P. Masson, R. Schweins et al., Pressure-induced molten globule state of human acetylcholinesterase: structural and dynamical changes monitored by neutron scattering, Physical Chemistry Chemical Physics, vol.134, issue.Suppl 5, pp.3157-3163, 2015.
DOI : 10.1021/ja3004655
URL : https://hal.archives-ouvertes.fr/hal-01148983

G. Weber and H. G. Drickamer, The effect of high pressure upon proteins and other biomolecules, Quarterly Reviews of Biophysics, vol.II, issue.01, pp.89-112, 1983.
DOI : 10.1038/259686a0

K. Heremans and L. Smeller, Protein structure and dynamics at high pressure, BBA)-Protein Structure and Molecular Enzymology, pp.353-370, 1998.
DOI : 10.1016/S0167-4838(98)00102-2

M. Erlkamp, J. Marion, N. Martinez, C. Czeslik, J. Peters et al., Influence of Pressure and Crowding on the Sub-Nanosecond Dynamics of Globular Proteins, The Journal of Physical Chemistry B, vol.119, issue.14, pp.4842-4848, 2015.
DOI : 10.1021/acs.jpcb.5b01017
URL : https://hal.archives-ouvertes.fr/hal-01162314

D. I. Svergun, M. V. Petoukhov, H. J. Michel, and . Koch, Determination of Domain Structure of Proteins from X-Ray Solution Scattering, Biophysical Journal, vol.80, issue.6, pp.2946-2953, 2001.
DOI : 10.1016/S0006-3495(01)76260-1

M. Ulmer, H. Herberhold, S. Fahsel, M. G. Ganzle, R. Winter et al., Effects of Pressure-Induced Membrane Phase Transitions on Inactivation of HorA, an ATP-Dependent Multidrug Resistance Transporter, in Lactobacillus plantarum, Applied and Environmental Microbiology, vol.68, issue.3, pp.1088-1095, 2002.
DOI : 10.1128/AEM.68.3.1088-1095.2002

F. Braganza and D. L. Worcester, Hydrostatic pressure induces hydrocarbon chain interdigitation in single-component phospholipid bilayers, Biochemistry, vol.25, issue.9, pp.2591-2596, 1986.
DOI : 10.1021/bi00357a047

K. Prasad, R. Shashidhar, B. P. Gaber, and S. C. Chandrasekhar, Pressure studies on two hydrated phospholipids ??? 1,2-dimyristoyl-phosphatidylcholine and 1,2-dipalmitoyl-phosphatidylcholine, Chemistry and Physics of Lipids, vol.43, issue.3, pp.227-235, 1987.
DOI : 10.1016/0009-3084(87)90010-7

C. Winter and . Jeworrek, Effect of pressure on membranes, Soft Matter, vol.254, issue.243, pp.3157-3173, 2009.
DOI : 10.1016/S0167-4838(01)00333-8

W. Winter, . Pilgrim, and . Ber, A SANS Study of High Pressure Phase Transitions in Model Biomembranes, Berichte der Bunsengesellschaft f??r physikalische Chemie, vol.37, issue.6, pp.708-717, 1989.
DOI : 10.1103/PhysRevA.37.3993

G. Ortore, F. Spinozzi, P. Mariani, A. Paciaroni, L. R. Barbosa et al., Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution, Journal of The Royal Society Interface, vol.12, issue.1, pp.619-634, 2009.
DOI : 10.1016/S0301-4622(02)00325-3

R. Doster and . Gebhardt, High pressure ??? unfolding of myoglobin studied by dynamic neutron scattering, Chemical Physics, vol.292, issue.2-3, pp.383-387, 2003.
DOI : 10.1016/S0301-0104(03)00064-8

R. A. Griepernau and . Böckmann, The Influence of 1-Alkanols and External Pressure on the Lateral Pressure Profiles of Lipid Bilayers, Biophysical Journal, vol.95, issue.12, pp.5766-5778, 2008.
DOI : 10.1529/biophysj.108.142125

C. Busch, L. C. Smuda, T. Pardo, and . Unruh, Molecular Mechanism of Long-Range Diffusion in Phospholipid Membranes Studied by Quasielastic Neutron Scattering, Journal of the American Chemical Society, vol.132, issue.10, pp.3232-3233, 2010.
DOI : 10.1021/ja907581s

D. Henzler-wildman and . Kern, Dynamic personalities of proteins, Nature, vol.124, issue.7172, pp.964-972, 2007.
DOI : 10.1038/nature06522
URL : http://www.nature.com/nature/journal/v450/n7172/pdf/nature06522.pdf

R. Kneller and K. Hinsen, Fractional Brownian dynamics in proteins, The Journal of Chemical Physics, vol.121, issue.20, pp.10278-10283, 2004.
DOI : 10.1021/ja00124a002
URL : https://hal.archives-ouvertes.fr/hal-00015422

R. Kneller, Quasielastic neutron scattering and relaxation processes in proteins: analytical and simulation-based models, Physical Chemistry Chemical Physics, vol.87, issue.8, pp.2641-2655, 2005.
DOI : 10.1103/PhysRev.136.A405
URL : https://hal.archives-ouvertes.fr/hal-00088607

F. Petrillo and . Sacchetti, Analysis of neutron diffraction data in the case of high-scattering cells. II. Complex cylindrical cells, Acta Crystallographica Section A Foundations of Crystallography, vol.48, issue.4, pp.508-515, 1992.
DOI : 10.1107/S0108767392000862

K. S. Rahman, A. Singwi, and . Sjölander, Theory of Slow Neutron Scattering by Liquids. I, Physical Review, vol.12, issue.3, pp.986-996, 1962.
DOI : 10.13182/NSE62-A26066

D. Gabel, U. Bicout, M. Lehnert, M. Tehei, G. Weik et al., Protein dynamics studied by neutron scattering, Quarterly Reviews of Biophysics, vol.35, issue.4, pp.327-367, 2003.
DOI : 10.1017/S0033583502003840

V. Réat, G. Zaccai, C. Ferrand, and C. Pfister, Functional Dynamics in Purple Membranes, 33 V. F. Sears, Neutron News, pp.26-37, 1992.

. Zaccai, Neutron scattering perspectives for protein dynamics, Journal of Non-Crystalline Solids, vol.357, issue.2, pp.615-621, 2011.
DOI : 10.1016/j.jnoncrysol.2010.06.060

B. Callen and T. A. Welton, Irreversibility and Generalized Noise, Physical Review, vol.19, issue.1, pp.34-40, 1951.
DOI : 10.1007/BF01327565

B. Z. Lipka, J. M. Chowdhry, and . Sturtevant, A comparison of the phase transition properties of 1,2-diacylphosphatidylcholines and 1,2-diacylphosphatidylethanolamines in water and deuterium oxide, The Journal of Physical Chemistry, vol.88, issue.22, pp.5401-5406, 1984.
DOI : 10.1021/j150666a058

R. Eisenblätter and . Winter, Pressure Effects on the Structure and Phase Behavior of DMPC-Gramicidin Lipid Bilayers: A Synchrotron SAXS and 2H-NMR Spectroscopy Study, Biophysical Journal, vol.90, issue.3, pp.956-966, 2006.
DOI : 10.1529/biophysj.105.069799

A. Bernsdorff, R. Wolf, E. Winter, and . Gratton, Effect of hydrostatic pressure on water penetration and rotational dynamics in phospholipid-cholesterol bilayers, Biophysical Journal, vol.72, issue.3, pp.1264-1277, 1997.
DOI : 10.1016/S0006-3495(97)78773-3

Y. Kucerka, N. Liu, H. I. Chu, S. Petrache, J. F. Tristram-nagle et al., Structure of Fully Hydrated Fluid Phase DMPC and DLPC Lipid Bilayers Using X-Ray Scattering from Oriented Multilamellar Arrays and from Unilamellar Vesicles, Biophysical Journal, vol.88, issue.4, pp.2626-2637, 2005.
DOI : 10.1529/biophysj.104.056606

F. Nagle and D. A. Wilkinson, Lecithin bilayers. Density measurement and molecular interactions, Biophysical Journal, vol.23, issue.2, pp.159-175, 1978.
DOI : 10.1016/S0006-3495(78)85441-1

G. Macdonald, A dilatometric investigation of the effects of general anaesthetics, alcohols and hydrostatic pressure on the phase transition in smectic mesophases of dipalmitoyl phosphatidylcholine, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.507, issue.1, pp.26-37, 1978.
DOI : 10.1016/0005-2736(78)90371-1

J. Nagy, S. Pieper, L. Krumova, M. Kovacs, G. Trapp et al., Dynamic properties of photosystem II membranes at physiological temperatures characterized by elastic incoherent neutron scattering. Increased flexibility associated with the inactivation of the oxygen evolving complex, Photosynthesis Research, vol.288, issue.12, pp.113-124, 2012.
DOI : 10.1126/science.288.5471.1604

J. Mikl, M. Peters, K. Trapp, W. J. Kornmueller, R. Schneider et al., Softness of Atherogenic Lipoproteins: A Comparison of Very Low Density Lipoprotein (VLDL) and Low Density Lipoprotein (LDL) Using Elastic Incoherent Neutron Scattering (EINS), Journal of the American Chemical Society, vol.133, issue.34, pp.13213-13215, 2011.
DOI : 10.1021/ja203679g

J. C. Meinhold, A. Smith, and A. H. Kitao, Picosecond fluctuating protein energy landscape mapped by pressure temperature molecular dynamics simulation, Proceedings of the National Academy of Sciences, vol.234, issue.4, pp.17261-17265, 2007.
DOI : 10.1006/jmbi.1993.1671
URL : http://www.pnas.org/content/104/44/17261.full.pdf

J. Peng and . Jonas, High-pressure phosphorus-31 NMR study of dipalmitoylphosphatidylcholine bilayers, Biochemistry, vol.31, issue.28, pp.6383-6390, 1992.
DOI : 10.1021/bi00143a004

A. Peng, J. Jonas, and . Jonas, High pressure 2H-NMR study of the order and dynamics of selectively deuterated dipalmitoyl phosphatidylcholine in multilamellar aqueous dispersions, Biophysical Journal, vol.68, issue.3, pp.1137-1144, 1995.
DOI : 10.1016/S0006-3495(95)80288-2

-. S. Lee, S. A. Mabry, A. Jonas, and J. Jonas, High-pressure proton NMR study of lateral self-diffusion of phosphatidylcholines in sonicated unilamellar vesicles, Chemistry and Physics of Lipids, vol.78, issue.2, pp.103-117, 1995.
DOI : 10.1016/0009-3084(95)02493-3

C. L. Jonas, A. Xie, P. J. Jonas, D. Grandinetti, D. Campbell et al., High-resolution 13C NMR study of pressure effects on the main phase transition in L-alpha-dipalmitoyl phosphatidylcholine vesicles., Proceedings of the National Academy of Sciences, vol.85, issue.12, pp.4115-4117, 1988.
DOI : 10.1073/pnas.85.12.4115

J. and A. Jonas, High-Pressure NMR Spectroscopy of Proteins and Membranes, Annual Review of Biophysics and Biomolecular Structure, vol.23, issue.1, pp.287-318, 1994.
DOI : 10.1146/annurev.bb.23.060194.001443

A. Eisenblätter, R. Zenerino, and . Winter, High-pressure1H NMR on model biomembranes: a study of the local anaesthetic tetracaine incorporated into POPC lipid bilayers, Magnetic Resonance in Chemistry, vol.93, issue.8, pp.662-667, 2000.
DOI : 10.1002/bbpc.19890930611

J. Roche, A. S. Ying, A. Maltsev, and . Bax, Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ??-Synuclein, ChemBioChem, vol.45, issue.14, pp.1754-1761, 2013.
DOI : 10.1016/j.polymer.2003.10.070

P. Paper, ;. W. References-folding, . Freeman, G. Weber, H. G. Drickamer et al., The Effect of High Pressure upon Proteins and Other Biomolecules Revisiting Volume Changes in Pressure-Induced Protein Unfolding Towards an Understanding of the Temperature/Pressure Configurational and Free-Energy Landscape of Biomolecules) Meersman, F.; Smeller, L.; Heremans, K. Protein Stability and Dynamics in the Pressure?Temperature Plane, Protein Science: A Guide 346?354. (6) Akasaka, K. Probing Conformational Fluctuation of Proteins by Pressure Perturbation, pp.9-112, 1595.

P. Suarez, M. C. Foguel, D. High-pressure, C. Biology, B. Mishra et al., Cold-and Pressure-Induced Dissociation of Protein Aggregates and Amyloid Fibrils High Hydrostatic Pressure Effects Investigated by Neutron Scattering on Lipid Multilamellar Vesicles Pressure-induced Molten Globule State of Human Acetylcholinesterase: Structural and Dynamical Changes Monitored by Neutron Scattering How Soft is a Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering, Conformational Substates in Proteins13) Meinhold, L.; Smith, J. C. Pressure-Dependent Transition in Protein Dynamics at about 4 kbar Revealed by Molecular Dynamics Simulation. Phys. Rev, pp.6518-6521, 1988.

X. , X. Meinhold, L. Smith, J. C. Kitao, A. Zewail et al., Picosecond Fluctuating Protein Energy Landscape Mapped by Pressure Temperature Molecular Dynamics Simulation, J. Phys. Chem. B Proc. Natl. Acad. Sci. U. S. A, vol.104, issue.14, pp.17261-17265, 2007.
DOI : 10.1073/pnas.0708199104
URL : http://www.pnas.org/content/104/44/17261.full.pdf

M. Funel, G. R. Kneller, V. Calandrini, and G. Kneller, Relaxation Dynamics of Lysozyme in Solution under Pressure: Combining Molecular Dynamics Simulations and Quasielastic Neutron Scattering Influence of Pressure on the Slow and Fast Fractional Relaxation Dynamics in Lysozyme: A Simulation Study, Chem. Phys. J. Chem. Phys, vol.345, issue.128, pp.289-297, 2008.

M. G. Ortore, F. Spinozzi, P. Mariani, A. Paciaroni, L. R. Barbosa et al., A Complementary Inelastic Neutron Scattering and Molecular Dynamics Simulation Study Combining Structure and Dynamics: Non-Denaturing High-Pressure Effect on Lysozyme in Solution (19) Daniel, I.; Oger, P.; Winter, R. Origins of Life and Biochemistry under High-Pressure Conditions, Influence of Pressure on the Low-Frequency Vibrational Modes of Lysozyme and Water, pp.326-340, 2006.

P. F. Mcmillan, . High-pressure, B. Biochemistry, A. P. Minton, and R. J. Ellis, How can Biochemical Reactions within Cells Differ from those in Test Tubes? J. Cell Sci Protein Misassembly: Macromolecular Crowding and Molecular Chaperones, S . ;G i e s ,H . ;W i n t e r ,R .P r o t e i n Encapsulation in Mesoporous Silicate: The Effects of Confinement on Protein Stability, Hydration, and Volumetric Properties. J. Am, pp.607-648, 2006.

. Chem, S. Soc-grobelny, and R. Winter, Crowding Effects on the Temperature and Pressure Dependent Structure, Stability and Folding Kinetics of Staphylococcal Nuclease, Nonlinear Pressure Dependence of the Interaction Potential of Dense Protein Solutions, 2004.

. Phys, . Rev, and J. Lett-mo?-ller, Reentrant Liquid-Liquid Phase Separation in Protein Solutions at Elevated Hydrostatic Pressures, Phys. Rev. Lett, vol.106, issue.112, pp.178102-178128, 2011.

M. Paulus, M. Tolan, R. Winter, J. Mo?-ller, M. A. Schroer et al., Exploring the Piezophilic Behavior of Natural Cosolvent Mixtures The Effect of Ionic Strength, Temperature, and Pressure on the Interaction Potential of Dense Protein Solutions: From Nonlinear Pressure Response to Protein Crystallization, Winter, R. Intermolecular Interactions in Highly Concentrated Protein Solutions upon Compression and the Role of the Solvent, pp.50-11413, 2011.

S. U. Egelhaaf, P. Schurtenberger, A. C. Dumetz, A. M. Chockla, E. W. Kaler et al., Equilibrium Cluster Formation in Concentrated Protein Solutions and Colloids Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid- Liquid Phase Separation, Gels, and Aggregates Macromolecular Crowding as a Suppressor of Human IAPP Fibril Formation and Cytotoxicity, 570?583. (32), pp.492-495, 2004.

M. Sztucki, H. Schober, T. Seydel, F. Schreiber, A. Stradner et al., Protein Self- Diffusion in Crowded Solutions Do Equilibrium Clusters Exist in Concentrated Lysozyme Solutions?, Proc. Natl. Acad. Sci. U. S. A. 2011, pp.11815-11820, 2008.

T. Narayanan, D. I. Svergun, L. Porcar, P. Falus, W. Chen et al., Formation of the Dynamic Clusters in Concentrated Lysozyme Protein Solutions Cluster-Driven Dynamical Arrest in Concentrated Lysozyme Solutions, Absence of Equilibrium Cluster Phase in Concentrated Lysozyme Solutions 126?129. (37), pp.5075-5080, 2008.

E. Fratini, K. Hong, P. Baglioni, F. Gabel, D. Bicout et al., Lysozyme Protein Solution with an Intermediate Range Order Structure Long-Time Mean-Square Displacements in Proteins, 327?367. (40) Vural, pp.7238-7247, 2002.

Z. Chowdhuri, R. B. Gregory, and A. P. Sokolov, Influence of Hydration on the Dynamics of Lysozyme, Biophys. J. Z, vol.91, issue.42, 2006.

M. Tyagi, H. Neill, Q. Zhang, A. P. Sokolov, J. C. Smith et al., Elastic and Conformational Softness of a Globular Protein Three Classes of Motion in the Dynamic Neutron-Scattering Susceptibility of a Globular Protein Surface Hydration Amplifies Single-Well Protein Atom Diffusion Propagating into the Macromolecular Core, Onori, G. Fast Fluctuations in Protein Powders: The Role of Hydration, pp.238102-754, 1989.

M. A. Gonzalez, B. Szalontai, G. Nagy, S. Krumova, E. Fodor et al., Thermal Behaviour of Hydrated Lysozyme in the Presence of Sucrose and Trehalose by EINS, Use of the Glass Electrode in Deuterium Oxide and the Relation Between the Standardized pD (paD) Scale and the Operational pH in Heavy Water50) Bouchoux, A.; Cayemitte, P.-E.; Jardin, pp.664-670, 1968.

B. Cabane, Casein Micelle Dispersions under Osmotic Stress, Biophys
URL : https://hal.archives-ouvertes.fr/hal-01454090

J. Steiner and R. F. , Reaction Volume of Protonic Ionization for Buffering Agent Prediction of Pressure Dependence of pH and pOH Structural Transitions of Lysozyme, J. Solution Chem. Biochim. Biophys. Acta S C, vol.96, issue.79, pp.715-725, 1964.

A. Cupane, A. Deriu, M. T. Di-bari, E. Farhi, and Y. Gerelli, XXX, XXX?XXX F Backscattering Spectrometer at ILL: Looking for Motions in Biological Macromolecules and Organisms. Neutron News, High Hydrostatic Pressure Equipment for Neutron Scattering Studies of Samples in Solutions. High Pressure Res. 2012, 32,9 7 ?102. (55) Sidorov, V. A.; Sadykov, R. A. Hydrostatic Limits of Fluorinert Liquids Used for Neutron and Transport Studies at High Pressure. J, pp.1-4, 2008.

P. Richard, D. Ferrand, M. Kearley, G. J. Rahman, A. Singwi et al., Analysis and Visualisation of Neutron-Scattering Data Theory of Slow Neutron Scattering by Liquids. I. Phys. Rev Fundamental and Biotechnological Applications of Neutron Scattering Measurements for Macromolecular Dynamics, 551?558. (59) Kharakoz, D. P. Protein Compressibility, Dynamics, and Pressure 511?525. (60) Soper, A. K. Structures of High-Density and Low-Density Water, pp.3005-3008, 1962.

E. Cupane, A. Fomina, M. Piazza, I. Peters, J. Schiro et al., Experimental Evidence for a Liquid-Liquid Crossover in Deeply Cooled Confined Water, 64) Zhai, Y.; Okoro, L.; Cooper, A.; Winter, R. Applications of Pressure Perturbation Calorimetry in Biophysical Studies. Biophys, pp.1808-1827, 2001.
DOI : 10.1063/1.2897826
URL : https://hal.archives-ouvertes.fr/hal-01131235

A. Isvoran, M. Cascante, and F. R. Mas, Effect of Crowding by Dextrans in Enzymatic Reactions, Biophys. Chem. A. V.; Medvedev, N. N, vol.20148, issue.18567, p.13

A. Geiger and A. Geiger, Calculation of the Volumetric Characteristics of Biomacromolecules in Solution by the Voronoi-Delaunay Technique, ?9. (68) Voloshin

R. Winter, F. M. Lauro, and D. H. Bartlett, Disentangling Volumetric and Hydrational Properties of Proteins, Prokaryotic Lifestyles in Deep Sea Habitats, pp.1881-1890, 2008.