Abstract
Neutron diffraction and spectroscopy were applied to describe the hydration and dynamics of a soluble protein and a natural membrane from extreme halophilic Archaea. The quantitative dependence of protein motions on water activity was clearly illustrated, and it was established that a minimum hydration shell is required for the systems to access their functional resilience, i.e. a dynamics state that allows biological activity.
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- Andreani C., Filabozzi A., Menzinger F., Desideri A., Deriu A., Di Cola D. Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering. Biophys J. 1995 Jun;68(6):2519–2523. doi: 10.1016/S0006-3495(95)80434-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bicout D. J., Zaccai G. Protein flexibility from the dynamical transition: a force constant analysis. Biophys J. 2001 Mar;80(3):1115–1123. doi: 10.1016/S0006-3495(01)76089-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bon C., Dianoux A. J., Ferrand M., Lehmann M. S. A model for water motion in crystals of lysozyme based on an incoherent quasielastic neutron-scattering study. Biophys J. 2002 Sep;83(3):1578–1588. doi: 10.1016/S0006-3495(02)73927-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bon C., Lehmann M. S., Wilkinson C. Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme. Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):978–987. doi: 10.1107/s0907444998018514. [DOI] [PubMed] [Google Scholar]
- Bonneté F., Madern D., Zaccaï G. Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions. J Mol Biol. 1994 Dec 9;244(4):436–447. doi: 10.1006/jmbi.1994.1741. [DOI] [PubMed] [Google Scholar]
- Cordone L., Ferrand M., Vitrano E., Zaccai G. Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biophys J. 1999 Feb;76(2):1043–1047. doi: 10.1016/S0006-3495(99)77269-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Daniel R. M., Finney J. L., Réat V., Dunn R., Ferrand M., Smith J. C. Enzyme dynamics and activity: time-scale dependence of dynamical transitions in glutamate dehydrogenase solution. Biophys J. 1999 Oct;77(4):2184–2190. doi: 10.1016/S0006-3495(99)77058-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Doster W., Cusack S., Petry W. Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature. 1989 Feb 23;337(6209):754–756. doi: 10.1038/337754a0. [DOI] [PubMed] [Google Scholar]
- Ferrand M., Dianoux A. J., Petry W., Zaccaï G. Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9668–9672. doi: 10.1073/pnas.90.20.9668. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fitter J. The temperature dependence of internal molecular motions in hydrated and dry alpha-amylase: the role of hydration water in the dynamical transition of proteins. Biophys J. 1999 Feb;76(2):1034–1042. doi: 10.1016/S0006-3495(99)77268-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gabel Frank, Bicout Dominique, Lehnert Ursula, Tehei Moeava, Weik Martin, Zaccai Giuseppe. Protein dynamics studied by neutron scattering. Q Rev Biophys. 2002 Nov;35(4):327–367. doi: 10.1017/s0033583502003840. [DOI] [PubMed] [Google Scholar]
- Grigorieff N., Ceska T. A., Downing K. H., Baldwin J. M., Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J Mol Biol. 1996 Jun 14;259(3):393–421. doi: 10.1006/jmbi.1996.0328. [DOI] [PubMed] [Google Scholar]
- Irimia Adriana, Ebel Christine, Madern Dominique, Richard Stéphane B., Cosenza Lawrence W., Zaccaï Giuseppe, Vellieux Frédéric M. D. The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. J Mol Biol. 2003 Feb 21;326(3):859–873. doi: 10.1016/s0022-2836(02)01450-x. [DOI] [PubMed] [Google Scholar]
- Lehnert U., Réat V., Weik M., Zaccaï G., Pfister C. Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes. Biophys J. 1998 Oct;75(4):1945–1952. doi: 10.1016/S0006-3495(98)77635-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Madern D., Ebel C., Zaccai G. Halophilic adaptation of enzymes. Extremophiles. 2000 Apr;4(2):91–98. doi: 10.1007/s007920050142. [DOI] [PubMed] [Google Scholar]
- Merzel Franci, Smith Jeremy C. Is the first hydration shell of lysozyme of higher density than bulk water? Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5378–5383. doi: 10.1073/pnas.082335099. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oesterhelt D. The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr Opin Struct Biol. 1998 Aug;8(4):489–500. doi: 10.1016/s0959-440x(98)80128-0. [DOI] [PubMed] [Google Scholar]
- Paciaroni A., Stroppolo M. E., Arcangeli C., Bizzarri A. R., Desideri A., Cannistraro S. Incoherent neutron scattering of copper azurin: a comparison with molecular dynamics simulation results. Eur Biophys J. 1999;28(6):447–456. doi: 10.1007/s002490050227. [DOI] [PubMed] [Google Scholar]
- Papadopoulos G., Dencher N. A., Zaccai G., Büldt G. Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway? J Mol Biol. 1990 Jul 5;214(1):15–19. doi: 10.1016/0022-2836(90)90140-h. [DOI] [PubMed] [Google Scholar]
- Parak F., Knapp E. W., Kucheida D. Protein dynamics. Mössbauer spectroscopy on deoxymyoglobin crystals. J Mol Biol. 1982 Oct 15;161(1):177–194. doi: 10.1016/0022-2836(82)90285-6. [DOI] [PubMed] [Google Scholar]
- Réat V., Dunn R., Ferrand M., Finney J. L., Daniel R. M., Smith J. C. Solvent dependence of dynamic transitions in protein solutions. Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9961–9966. doi: 10.1073/pnas.97.18.9961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Svergun D. I., Richard S., Koch M. H., Sayers Z., Kuprin S., Zaccai G. Protein hydration in solution: experimental observation by x-ray and neutron scattering. Proc Natl Acad Sci U S A. 1998 Mar 3;95(5):2267–2272. doi: 10.1073/pnas.95.5.2267. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tehei Moeava, Franzetti Bruno, Madern Dominique, Ginzburg Margaret, Ginzburg Ben Z., Giudici-Orticoni Marie-Thérèse, Bruschi Mireille, Zaccai Giuseppe. Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering. EMBO Rep. 2004 Jan;5(1):66–70. doi: 10.1038/sj.embor.7400049. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tehei Moeava, Franzetti Bruno, Maurel Marie-Christine, Vergne Jacques, Hountondji Codjo, Zaccai Giuseppe. The search for traces of life: the protective effect of salt on biological macromolecules. Extremophiles. 2002 May 28;6(5):427–430. doi: 10.1007/s00792-002-0275-6. [DOI] [PubMed] [Google Scholar]
- Tournier Alexander L., Xu Jiancong, Smith Jeremy C. Translational hydration water dynamics drives the protein glass transition. Biophys J. 2003 Sep;85(3):1871–1875. doi: 10.1016/S0006-3495(03)74614-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zaccai G., Gilmore D. J. Areas of hydration in the purple membrane of Halobacterium halobium: a neutron diffraction study. J Mol Biol. 1979 Aug 5;132(2):181–191. doi: 10.1016/0022-2836(79)90390-5. [DOI] [PubMed] [Google Scholar]
- Zaccai G. How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science. 2000 Jun 2;288(5471):1604–1607. doi: 10.1126/science.288.5471.1604. [DOI] [PubMed] [Google Scholar]
- Zaccai G. Structure and hydration of purple membranes in different conditions. J Mol Biol. 1987 Apr 5;194(3):569–572. doi: 10.1016/0022-2836(87)90683-8. [DOI] [PubMed] [Google Scholar]
