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Volumn 35, Issue 4, 2002, Pages 327-367

Protein dynamics studied by neutron scattering

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; SOLVENT;

EID: 0036880187     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0033583502003840     Document Type: Review
Times cited : (300)

References (104)
  • 1
    • 33751155047 scopus 로고
    • Enzymes from microorganisms in extreme environments
    • ADAMS, M. W. W. & KELLY, R. M. (1995). Enzymes from microorganisms in extreme environments. Chem. Engng News 18, 32-42.
    • (1995) Chem. Engng. News , vol.18 , pp. 32-42
    • Adams, M.W.W.1    Kelly, R.M.2
  • 2
    • 0029061330 scopus 로고
    • Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering
    • ANDREANI, C., FILABOZZI, A., MENZINGER, F., DESIDERI, A., DERIU, A. & DI COLA, D. (1995). Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering. Biophys. J. 68, 2519-2523.
    • (1995) Biophys. J. , vol.68 , pp. 2519-2523
    • Andreani, C.1    Filabozzi, A.2    Menzinger, F.3    Desideri, A.4    Deriu, A.5    Di Cola, D.6
  • 3
    • 0009071257 scopus 로고
    • Formation of glasses from liquids and biopolymers
    • ANGELL, C. A. (1995). Formation of glasses from liquids and biopolymers. Science 267, 1924-1935.
    • (1995) Science , vol.267 , pp. 1924-1935
    • Angell, C.A.1
  • 6
    • 2742571585 scopus 로고    scopus 로고
    • Slow dynamics of water molecules on the surface of a globular protein
    • BELLISSENT-FUNEL, M. C., ZANOTTI, J. M. & CHEN, S. H. (1996). Slow dynamics of water molecules on the surface of a globular protein. Faraday Discuss. 103, 281-294.
    • (1996) Faraday Discuss. , vol.103 , pp. 281-294
    • Bellissent-Funel, M.C.1    Zanotti, J.M.2    Chen, S.H.3
  • 7
    • 0035118232 scopus 로고    scopus 로고
    • Protein flexibility from the dynamical transition: A force constant analysis
    • BICOUT, D.J. & ZACCAI, G. (2001). Protein flexibility from the dynamical transition: a force constant analysis. Biopbys. J. 80, 1115-1123.
    • (2001) Biopbys. J. , vol.80 , pp. 1115-1123
    • Bicout, D.J.1    Zaccai, G.2
  • 8
    • 0034773304 scopus 로고    scopus 로고
    • Low-frequency vibrational modes in proteins: A neutron scattering investigation
    • BIZZARRI, A.R., PACIARONI, A., ARCANGELI, C. & CANNISTRARO, S. (2001). Low-frequency vibrational modes in proteins: a neutron scattering investigation. Eur Biophys. J. 30, 443-449.
    • (2001) Eur Biophys. J. , vol.30 , pp. 443-449
    • Bizzarri, A.R.1    Paciaroni, A.2    Arcangeli, C.3    Cannistraro, S.4
  • 10
    • 0036708465 scopus 로고    scopus 로고
    • A model for water motion in crystals of lysozyme based on an incoherent quasi-elastic neutron scattering study
    • BON, C., DIANOUX, A. J., FERRAND, M. & LEHMANN, M. S. (2002). A model for water motion in crystals of lysozyme based on an incoherent quasi-elastic neutron scattering study. Biophys. J. 83, 1578-1588.
    • (2002) Biophys. J. , vol.83 , pp. 1578-1588
    • Bon, C.1    Dianoux, A.J.2    Ferrand, M.3    Lehmann, M.S.4
  • 11
    • 0033135301 scopus 로고    scopus 로고
    • QuasiLaue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme
    • BON, C., LEHMANN, M. S. & WILKINSON, C. (1999). QuasiLaue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme. Acta Crystallogr. (D) 55, 978-987.
    • (1999) Acta Crystallogr. (D) , vol.55 , pp. 978-987
    • Bon, C.1    Lehmann, M.S.2    Wilkinson, C.3
  • 12
    • 0028034679 scopus 로고
    • Stability against denaturation mechanisms in halophilic malate dehydrogenase 'adapt' to solvent conditions
    • BONNETÉ, F., MADERN, D. & ZACCAI, G. (1994). Stability against denaturation mechanisms in halophilic malate dehydrogenase 'adapt' to solvent conditions. J. molec. Biol. 244, 436-447.
    • (1994) J. Molec. Biol. , vol.244 , pp. 436-447
    • Bonneté, F.1    Madern, D.2    Zaccai, G.3
  • 13
    • 0035965129 scopus 로고    scopus 로고
    • Dynamic regimes and correlated structural dynamics in native and denatured α-lactalbumin
    • BU, Z., COOK, J. & CALLAWAY, J. E. (2001). Dynamic regimes and correlated structural dynamics in native and denatured α-lactalbumin. J. molec. Biol. 312, 865-873.
    • (2001) J. Molec. Biol. , vol.312 , pp. 865-873
    • Bu, Z.1    Cook, J.2    Callaway, J.E.3
  • 14
    • 0034636990 scopus 로고    scopus 로고
    • A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering
    • BU, Z., NEUMANN, D. A., LEE, S.-H., BROWN, C. M., ENGELMAN D. M. & HAN, C. C. (2000). A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering. J. molec. Biol. 301, 525-536.
    • (2000) J. Molec. Biol. , vol.301 , pp. 525-536
    • Bu, Z.1    Neumann, D.A.2    Lee, S.-H.3    Brown, C.M.4    Engelman, D.M.5    Han, C.C.6
  • 15
    • 0032554626 scopus 로고    scopus 로고
    • Protein folding dynamics: Quantitative comparison between theory and experiment
    • BURTON, R. E., MYERS, J. K. & OAS, T. G. (1998). Protein folding dynamics: quantitative comparison between theory and experiment. Biochemistry 37, 5337-5343.
    • (1998) Biochemistry , vol.37 , pp. 5337-5343
    • Burton, R.E.1    Myers, J.K.2    Oas, T.G.3
  • 16
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • CHAN, H. S. & DILL, K. A. (1998). Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics. Proteins: Struct., Funct. Genet. 30, 2-33.
    • (1998) Proteins: Struct., Funct. Genet. , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 18
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    • CORDONE, L., FERRAND, M., VITRANO, E. & ZACCAI, G. (1999). Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biopbys. J. 76, 1043-1047.
    • (1999) Biopbys. J. , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 19
    • 0031889847 scopus 로고    scopus 로고
    • A reduction of protein specific motions in Co-ligated myoglobin embedded in a trehalose glass
    • CORDONE, L., GALADJA, P., VITRANO, E., GASSMANN, A., OSTERMANN, A. & PARAK, F. (1998). A reduction of protein specific motions in Co-ligated myoglobin embedded in a trehalose glass. Eur. Biophys. J. 27, 173-176.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 173-176
    • Cordone, L.1    Galadja, P.2    Vitrano, E.3    Gassmann, A.4    Ostermann, A.5    Parak, F.6
  • 20
    • 0032863425 scopus 로고    scopus 로고
    • Enzyme dynamics and activity: Time-scale dependence of dynamical transitions in glutamate dehydrogenase solution
    • DANIEL, R. M., FINNEY, J. L., RÉAT, V., DUNN, R., FERRAND, M., SMITH, J. C., DUNN, R. V. & FINNEY, J. (1999). Enzyme dynamics and activity: time-scale dependence of dynamical transitions in glutamate dehydrogenase solution. Biophys. J. 77, 2184-2190.
    • (1999) Biophys. J. , vol.77 , pp. 2184-2190
    • Daniel, R.M.1    Finney, J.L.2    Réat, V.3    Dunn, R.4    Ferrand, M.5    Smith, J.C.6    Dunn, R.V.7    Finney, J.8
  • 21
    • 0035826241 scopus 로고    scopus 로고
    • Super-cooled liquids and the glass transition
    • DEBENEDETII, P. G. & STILLINGER, F. H. (2001). Super-cooled liquids and the glass transition. Nature 410, 259-267.
    • (2001) Nature , vol.410 , pp. 259-267
    • Debenedetii, P.G.1    Stillinger, F.H.2
  • 23
    • 0030862281 scopus 로고    scopus 로고
    • Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering
    • DIEHL, M., DOSTER, W., PETRY, W. & SCHOBER, H. (1997). Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering. Biophys. J. 73, 2726-2732.
    • (1997) Biophys. J. , vol.73 , pp. 2726-2732
    • Diehl, M.1    Doster, W.2    Petry, W.3    Schober, H.4
  • 24
    • 0028466243 scopus 로고
    • Protein folding. Solid evidence for molten globules
    • DOBSON, C. M. (1994). Protein folding. Solid evidence for molten globules. Curr. Sci. 4, 636-640.
    • (1994) Curr. Sci. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 25
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • DOIG, A. J. & STERNBERG, M.J. (1995). Side-chain conformational entropy in protein folding. Protein Sci. 4 2247-2251.
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.2
  • 26
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • DOSTER, W., CUSACK, S. & PETRY, W. (1989). Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature 337, 754-756.
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 27
    • 0001706226 scopus 로고
    • Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering
    • DOSTER, W., CUSACK, S. & PETRY, W. (1990). Dynamic instability of liquidlike motions in a globular protein observed by inelastic neutron scattering. Phys. Rev. Lett. 65, 1080-1083.
    • (1990) Phys. Rev. Lett. , vol.65 , pp. 1080-1083
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 28
    • 0001890328 scopus 로고
    • Sul moto dei neutroni nelle sostanze idrogenate
    • FERMI, E. (1936). Sul moto dei neutroni nelle sostanze idrogenate. La Ricerca Scientifica 7, 13-52.
    • (1936) La Ricerca Scientifica , vol.7 , pp. 13-52
    • Fermi, E.1
  • 29
    • 0027491027 scopus 로고
    • Thermal motions and function of bacterio-rhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • FERRAND, M., DIANOUX, A. J., PETRY, W. & ZACCAI, G. (1993a). Thermal motions and function of bacterio-rhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proc. natn. Acad. Sci. USA 90, 9668-9672.
    • (1993) Proc. Natn. Acad. Sci. USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 30
    • 0013319758 scopus 로고
    • Dynamical transition of bacteriorhodopsin in purple membranes revealed by neutron scattering: A relation between structure, dynamics and function
    • FERRAND, M., PETRY, W., DIANOUX, A. J. & ZACCAI, G. (1993b). Dynamical transition of bacteriorhodopsin in purple membranes revealed by neutron scattering: a relation between structure, dynamics and function. Physica A 201, 524-529.
    • (1993) Physica A , vol.201 , pp. 524-529
    • Ferrand, M.1    Petry, W.2    Dianoux, A.J.3    Zaccai, G.4
  • 31
    • 0000015526 scopus 로고
    • Defect activity in amorphous ice from isotopic exchange data: Insight into the glass transition
    • FISHER, M. & DEVLIN, J. P. (1995). Defect activity in amorphous ice from isotopic exchange data: insight into the glass transition. J. Phys. Chem. 99, 11584-11590.
    • (1995) J. Phys. Chem. , vol.99 , pp. 11584-11590
    • Fisher, M.1    Devlin, J.P.2
  • 32
    • 0033064923 scopus 로고    scopus 로고
    • The temperature dependence of internal molecular motions in hydrated and dry alpha-amylase: The role of hydration water in the dynamical transition of proteins
    • FITTER, J. (1999). 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. 76, 1034-1042.
    • (1999) Biophys. J. , vol.76 , pp. 1034-1042
    • Fitter, J.1
  • 33
    • 0031712270 scopus 로고    scopus 로고
    • Molecular motions and hydration of purple membranes and disk membranes studied by neutron scattering
    • FITTER, J., ERNST, O. P., HAUSS, T., LECHNER, R. E., HOFMANN, K. P. & DENCHER, N. A. (1998a). Molecular motions and hydration of purple membranes and disk membranes studied by neutron scattering. Eur. Biophys. J. 27, 638-645.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 638-645
    • Fitter, J.1    Ernst, O.P.2    Hauss, T.3    Lechner, R.E.4    Hofmann, K.P.5    Dencher, N.A.6
  • 34
    • 0033865067 scopus 로고    scopus 로고
    • Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase
    • FITTER, J. & HEBERLE, J. (2000). Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase. Biophys. J. 79, 1629-1636.
    • (2000) Biophys. J. , vol.79 , pp. 1629-1636
    • Fitter, J.1    Heberle, J.2
  • 35
    • 0035807038 scopus 로고    scopus 로고
    • Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: Mechanisms of thermal adaptation
    • FITTER, J., HERMANN, R., DENCHER, N. A., BLUME, A. & HAUSS, T. (2001). Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation. Biochemistry 40, 10723-10731.
    • (2001) Biochemistry , vol.40 , pp. 10723-10731
    • Fitter, J.1    Hermann, R.2    Dencher, N.A.3    Blume, A.4    Hauss, T.5
  • 36
    • 0029836757 scopus 로고    scopus 로고
    • Internal molecular motions of bacterio-rhodopsin: Hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes
    • FITTER, J., LECHNER, R. E., BÜLDT, G. & DENCHER, N. A. (1996a). Internal molecular motions of bacterio-rhodopsin: hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes. Proc. natn. Acad. Sci. USA 93, 7600-7605.
    • (1996) Proc. Natn. Acad. Sci. USA , vol.93 , pp. 7600-7605
    • Fitter, J.1    Lechner, R.E.2    Büldt, G.3    Dencher, N.A.4
  • 37
    • 0013263799 scopus 로고    scopus 로고
    • Influence of lipids on the dynamical behaviour of bacteriorhodopsin in the purple membrane
    • eds. S. Cusack, H. Büttner, M. Ferrand, P. Langan & P. Timmins. Grenoble: Adenine Press
    • FITTER, J., LECHNER, R. E. & DENCHER, N. A. (1996b). Influence of lipids on the dynamical behaviour of bacteriorhodopsin in the purple membrane. In Biological Macromolecular Dynamics (eds. S. Cusack, H. Büttner, M. Ferrand, P. Langan & P. Timmins), pp. 123-127. Grenoble: Adenine Press.
    • (1996) Biological Macromolecular Dynamics , pp. 123-127
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 38
    • 0030217736 scopus 로고    scopus 로고
    • Temperature dependence of molecular motions in the membrane protein bacteriorhodopsin from QINS
    • FITTER, J., LECHNER, R. E. & DENCHER, N. A. (1996c). Temperature dependence of molecular motions in the membrane protein bacteriorhodopsin from QINS. Physica (B) 226, 61-65.
    • (1996) Physica (B) , vol.226 , pp. 61-65
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 39
    • 0030823236 scopus 로고    scopus 로고
    • Pico-second molecular motions in bacteriorhodopsin from neutron scattering
    • FITTER, J., LECHNER, R. E. & DENCHER, N. A. (1997). Pico-second molecular motions in bacteriorhodopsin from neutron scattering. Biophys. J. 73, 2126-2137.
    • (1997) Biophys. J. , vol.73 , pp. 2126-2137
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 40
    • 0032657118 scopus 로고    scopus 로고
    • Bacteriorhodopsin and rhodopsin studied by incoherent neutron scattering: Dynamical properties of ground states and light activated intermediates
    • FITTER, J., VERCLAS, S. A., LECHNER, R. E., BUELDT, G., ERNST, O. P., HOFMANN, K. P. & DENCHER, N. A. (1999). Bacteriorhodopsin and rhodopsin studied by incoherent neutron scattering: dynamical properties of ground states and light activated intermediates. Physica (B) 266, 35-40.
    • (1999) Physica (B) , vol.266 , pp. 35-40
    • Fitter, J.1    Verclas, S.A.2    Lechner, R.E.3    Bueldt, G.4    Ernst, O.P.5    Hofmann, K.P.6    Dencher, N.A.7
  • 41
    • 0032555351 scopus 로고    scopus 로고
    • Function and picosecond dynamics of bacteriorhodopsin in purple membrane at different lipidation and hydration
    • FITTER, J., VERCLAS, S. A., LECHNER, R. E., SEELERT, H. & DENCHER, N. A. (1998b). Function and picosecond dynamics of bacteriorhodopsin in purple membrane at different lipidation and hydration. FEBS Lett. 433, 321-325.
    • (1998) FEBS Lett. , vol.433 , pp. 321-325
    • Fitter, J.1    Verclas, S.A.2    Lechner, R.E.3    Seelert, H.4    Dencher, N.A.5
  • 42
    • 0013220338 scopus 로고    scopus 로고
    • Neutron spectroscopy by time-of-flight, backscattering and spin-echo techniques
    • (eds. R. Pike & P. Sabatier). San Diego, San Francisco, New York, Boston, London, Sydney, Tokyo: Academic Press
    • FRICK, B. & FARAGO, B. (2002). Neutron spectroscopy by time-of-flight, backscattering and spin-echo techniques. In Scattering: Scattering and Inverse Scattering in Pure and Applied Science (eds. R. Pike & P. Sabatier), pp. 1209-1241. San Diego, San Francisco, New York, Boston, London, Sydney, Tokyo: Academic Press.
    • (2002) Scattering: Scattering and Inverse Scattering in Pure and Applied Science , pp. 1209-1241
    • Frick, B.1    Farago, B.2
  • 43
    • 0032975368 scopus 로고    scopus 로고
    • Anisotropic motion of cholesterol in oriented DPPC bilayers studied by quasielastic neutron scattering: The liquid-oriented phase
    • GLISS, C., RANDEL, O., CASALTA, H., SACKMANN, E., ZORN, R. & BAYERL, T. (1999). Anisotropic motion of cholesterol in oriented DPPC bilayers studied by quasielastic neutron scattering: The liquid-oriented phase. Biophys. J. 77, 331-340.
    • (1999) Biophys. J. , vol.77 , pp. 331-340
    • Gliss, C.1    Randel, O.2    Casalta, H.3    Sackmann, E.4    Zorn, R.5    Bayerl, T.6
  • 44
    • 0004986545 scopus 로고
    • Relaxation processes in supercooled liquids
    • GÖTZE, W. & SJÖGREN, L. (1992). Relaxation processes in supercooled liquids. Rep. Prog. Phys. 55, 241-376.
    • (1992) Rep. Prog. Phys. , vol.55 , pp. 241-376
    • Götze, W.1    Sjögren, L.2
  • 45
    • 0033053602 scopus 로고    scopus 로고
    • Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin
    • GRIKO, Y. V. & REMETA, D.P. (1999). Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin. Protein Sci. 8, 554-561.
    • (1999) Protein Sci. , vol.8 , pp. 554-561
    • Griko, Y.V.1    Remeta, D.P.2
  • 48
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • JAENICKE, R. (2000). Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc. natn. Acad. Sci. USA 97, 2962-2964.
    • (2000) Proc. Natn. Acad. Sci. USA , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 49
    • 0000901912 scopus 로고
    • The glass-liquid transition of hyperquenched water
    • JOHARI, G. P., HALLBRUCKER, A. & MAYER, E. (1987). The glass-liquid transition of hyperquenched water. Nature 330, 552-553.
    • (1987) Nature , vol.330 , pp. 552-553
    • Johari, G.P.1    Hallbrucker, A.2    Mayer, E.3
  • 50
    • 0000241921 scopus 로고
    • Super-cooling of water to - 92 °C under pressure
    • KANNO, H., SPEEDY, R.J. & ANGELL, C. A. (1975). Super- cooling of water to - 92 °C under pressure. Science 189, 880-881.
    • (1975) Science , vol.189 , pp. 880-881
    • Kanno, H.1    Speedy, R.J.2    Angell, C.A.3
  • 51
    • 0028327236 scopus 로고
    • Protein folding dynamics: The diffusion-collision model and experimental data
    • KARPLUS, M. & WEAVER, D. L. (1994). Protein folding dynamics: the diffusion-collision model and experimental data. Protein Sci. 3, 650-668.
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 52
    • 0029001090 scopus 로고
    • Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
    • KLEFHABER, T., LABHARDT, A. M. & BALDWIN, R. L. (1995). Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375, 513-515.
    • (1995) Nature , vol.375 , pp. 513-515
    • Klefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 53
    • 0028100759 scopus 로고
    • Liquid-like side-chain dynamics in myoglobin
    • KNELLER, G. R. & SMITH, J. C. (1994). Liquid-like side-chain dynamics in myoglobin. J. molec. Biol. 242, 181-185.
    • (1994) J. Molec. Biol. , vol.242 , pp. 181-185
    • Kneller, G.R.1    Smith, J.C.2
  • 54
    • 0028950931 scopus 로고
    • Hydration dependence of chain dynamics and local diffusion in L-α-dipalmitoylphosphatidylcholine multilayers studied by incoherent quasielastic neutron scattering
    • KÖNIG, S., BAYERL, T. M., CODDENS, G., RICHTER, D. & SACKMANN, E. (1995). Hydration dependence of chain dynamics and local diffusion in L-α-dipalmitoylphosphatidylcholine multilayers studied by incoherent quasielastic neutron scattering. Biophys. J. 68, 1871-1880.
    • (1995) Biophys. J. , vol.68 , pp. 1871-1880
    • König, S.1    Bayerl, T.M.2    Coddens, G.3    Richter, D.4    Sackmann, E.5
  • 55
    • 0001273751 scopus 로고
    • Molecular dynamics of lipid bilayers studied by incoherent quasi-elastic neutron scattering
    • KÖNIG, S., PFEIFFER, W., BAYERL, T. M., RICHTER, D. & SACKMANN, E. (1992). Molecular dynamics of lipid bilayers studied by incoherent quasi-elastic neutron scattering. Journal de Physique II 2, 1589-1615.
    • (1992) Journal de Physique II , vol.2 , pp. 1589-1615
    • König, S.1    Pfeiffer, W.2    Bayerl, T.M.3    Richter, D.4    Sackmann, E.5
  • 56
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • KUNTZ, JR., I. D. & KAUZMANN, W. (1974). Hydration of proteins and polypeptides. ADV. Protein. Chem. 28, 239-345.
    • (1974) ADV. Protein. Chem. , vol.28 , pp. 239-345
    • Kuntz I.D., Jr.1    Kauzmann, W.2
  • 57
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of alpha-lactalbumin
    • KUWAJIMA, K. (1996). The molten globule state of alpha-lactalbumin. FASEB J. 10, 102-109.
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 58
    • 0013282951 scopus 로고
    • Proton dynamics in a 2D-'Single Crystal' of bactetiorhodopsin
    • LECHNER, R. E., DENCHER, N. A., FITTER, J. & BÜLDT, G. (1992). Proton dynamics in a 2D-'Single Crystal' of bactetiorhodopsin. Physica Scripta T45, 236-241.
    • (1992) Physica Scripta T , vol.45 , pp. 236-241
    • Lechner, R.E.1    Dencher, N.A.2    Fitter, J.3    Büldt, G.4
  • 59
    • 0032478520 scopus 로고    scopus 로고
    • Dehydration of biological membranes by cooling: An investigation on the purple membrane
    • LECHNER, R. E., FITTER, J., DENCHER, N. A. & HAUSS, T. (1998). Dehydration of biological membranes by cooling: an investigation on the purple membrane. J. molec. Biol. 277, 593-603.
    • (1998) J. Molec. Biol. , vol.277 , pp. 593-603
    • Lechner, R.E.1    Fitter, J.2    Dencher, N.A.3    Hauss, T.4
  • 60
    • 0344863187 scopus 로고    scopus 로고
    • Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: Correlation with kinetics and light-induced conformational changes
    • LEHNERT, U., RÉAT, V., WEIK, M., ZACCAI, G. & PFISTER, C. (1998). Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes. Biophys. J. 75, 1945-1952.
    • (1998) Biophys. J. , vol.75 , pp. 1945-1952
    • Lehnert, U.1    Réat, V.2    Weik, M.3    Zaccai, G.4    Pfister, C.5
  • 61
    • 0014407981 scopus 로고
    • Multilayers of phospholipid bimolecular leaflets
    • LEVINE, Y. K., BAILEY, A. I. & WILKINS, M. H. (1968). Multilayers of phospholipid bimolecular leaflets. Nature 220, 577-578.
    • (1968) Nature , vol.220 , pp. 577-578
    • Levine, Y.K.1    Bailey, A.I.2    Wilkins, M.H.3
  • 63
    • 0001556207 scopus 로고
    • Observations of elastic and quasi-elastic nuclear gamma resonance absorption in hemoglobin crystals
    • MAYO, K. H., PARAK, F. & MÖSSBAUER, R. L. (1981). Observations of elastic and quasi-elastic nuclear gamma resonance absorption in hemoglobin crystals. Phys. Lett. 82A, 468-470.
    • (1981) Phys. Lett. , vol.82 A , pp. 468-470
    • Mayo, K.H.1    Parak, F.2    Mössbauer, R.L.3
  • 64
    • 0030004479 scopus 로고    scopus 로고
    • Structural fluctuations of myoglobin from normal-modes, Mössbauer, Raman and absorption spectroscopy
    • MELCHERS, B., KNAPP, E. W., PARAK, F., CORDONE, L., CUPANE, A. & LEONE, M. (1996). Structural fluctuations of myoglobin from normal-modes, Mössbauer, Raman and absorption spectroscopy. Biophys. J. 70, 2092-2099.
    • (1996) Biophys. J. , vol.70 , pp. 2092-2099
    • Melchers, B.1    Knapp, E.W.2    Parak, F.3    Cordone, L.4    Cupane, A.5    Leone, M.6
  • 65
    • 0017383022 scopus 로고
    • Malate dehydrogenase isolated from extremly halophilic bacteria of the Dead Sea. 2. Effect of salt on catalytic activity and structure
    • MEVARECH, M. & NEUMANN, E. (1977). Malate dehydrogenase isolated from extremly halophilic bacteria of the Dead Sea. 2. Effect of salt on catalytic activity and structure. Biochemistry 16, 3786-3792.
    • (1977) Biochemistry , vol.16 , pp. 3786-3792
    • Mevarech, M.1    Neumann, E.2
  • 66
    • 0025811817 scopus 로고
    • Lysozyme and alpha-lactalbumin: Structure, function and inter-relationships
    • MCKENZIE, H. A. & WHITE, JR., F. H. (1991). Lysozyme and alpha-lactalbumin: structure, function and inter-relationships. Adv. Protein Chem. 41, 173-315.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 173-315
    • Mckenzie, H.A.1    White F.H., Jr.2
  • 67
    • 33750525203 scopus 로고
    • Vitreous ice: Irreversible transformations during warm-up
    • MCMILLAN, J. A. & Los, S. C. (1965). Vitreous ice: irreversible transformations during warm-up. Nature 206, 806-807.
    • (1965) Nature , vol.206 , pp. 806-807
    • Mcmillan, J.A.1    Los, S.C.2
  • 69
    • 0032569809 scopus 로고    scopus 로고
    • The relationship between liquid, supercooled and glassy water
    • MISHIMA, A. & STANLEY, H. E. (1998). The relationship between liquid, supercooled and glassy water. Nature 396, 329-335.
    • (1998) Nature , vol.396 , pp. 329-335
    • Mishima, A.1    Stanley, H.E.2
  • 70
    • 0000288095 scopus 로고
    • Structure of water and hydrophobic bonding in proteins. IV. The thermodynamic properties of lipid deuterium oxide
    • NEMETHY, G. & SCHERAGA, H. A. (1964). Structure of water and hydrophobic bonding in proteins. IV. The thermodynamic properties of lipid deuterium oxide. J. chem. Phys. 41, 680-689.
    • (1964) J. Chem. Phys. , vol.41 , pp. 680-689
    • Nemethy, G.1    Scheraga, H.A.2
  • 71
    • 0035819192 scopus 로고    scopus 로고
    • Low-frequency vibrational anomalies in β-lactoglobulin: Contribution of different hydrogen classes revealed by inelastic neutron scattering
    • ORECCHINI, A., PACIARONI, A., BIZZARRI, A. R. & CANNISTRARO, S. (2001). Low-frequency vibrational anomalies in β-lactoglobulin: contribution of different hydrogen classes revealed by inelastic neutron scattering. J. phys. Chem. (B) 105, 12150-12156.
    • (2001) J. Phys. Chem. (B) , vol.105 , pp. 12150-12156
    • Orecchini, A.1    Paciaroni, A.2    Bizzarri, A.R.3    Cannistraro, S.4
  • 72
    • 0022590625 scopus 로고
    • Intracellular salt concentrations of the anaetobic halophilic eubacteria Haloanaerobium praevalens and Halobacteroides halobius
    • OREN, A. (1986). Intracellular salt concentrations of the anaetobic halophilic eubacteria Haloanaerobium praevalens and Halobacteroides halobius. Can. J. Microbiol. 32, 4-9.
    • (1986) Can. J. Microbiol. , vol.32 , pp. 4-9
    • Oren, A.1
  • 73
  • 75
    • 0020333863 scopus 로고
    • Protein dynamics: Mösssbauer spectroscopy on deoxymyoglobin crystals
    • PARAK, F., KNAPP, E. W. & KUCHEIDA, D. (1982). Protein dynamics: Mösssbauer spectroscopy on deoxymyoglobin crystals. J. molec. Biol. 161, 177-194.
    • (1982) J. Molec. Biol. , vol.161 , pp. 177-194
    • Parak, F.1    Knapp, E.W.2    Kucheida, D.3
  • 76
    • 0043194670 scopus 로고    scopus 로고
    • Evolution of the internal dynamics of two globular proteins from dry powder to solution
    • PÉREZ, J., ZANOTTI, J. M. & DURANI, D. (1999). Evolution of the internal dynamics of two globular proteins from dry powder to solution. Biophys. J. 77, 454-469.
    • (1999) Biophys. J. , vol.77 , pp. 454-469
    • Pérez, J.1    Zanotti, J.M.2    Durani, D.3
  • 77
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • PTITSSYN, O. B. (1995). Molten globule and protein folding. Adv. Protein Chem. 47, 83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitssyn, O.B.1
  • 78
    • 0035868526 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics
    • PORTMAN, J. J., TAKADA, S. & WOLYNES, P. G. (2001). Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics. J. chem. Phys. 114, 5082-5096.
    • (2001) J. Chem. Phys. , vol.114 , pp. 5082-5096
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 81
    • 0002943198 scopus 로고    scopus 로고
    • Functional dynamics in purple membrane
    • eds. S. Cusack, H. Büttner, M. Ferrand, P. Langan & P. Timmins. Schenectady, NY, USA: Adenine Press
    • RÉAT, V., ZACCAI, G., FERRAND, M. & PFISTER, C. (1997). Functional dynamics in purple membrane. In Biological Macromolecullar Dynamics (eds. S. Cusack, H. Büttner, M. Ferrand, P. Langan & P. Timmins), pp. 117-122. Schenectady, NY, USA: Adenine Press.
    • (1997) Biological Macromolecullar Dynamics , pp. 117-122
    • Réat, V.1    Zaccai, G.2    Ferrand, M.3    Pfister, C.4
  • 82
    • 0030927638 scopus 로고    scopus 로고
    • Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering
    • RECEVEUR, V., CALMETTES, P., SMITH, J. C., DESMADRIL, M., CODDENS, G. & DURAND, D. (1997). Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering. Proteins: Struct., Funct. Genet. 28, 380-387.
    • (1997) Proteins: Struct., Funct. Genet. , vol.28 , pp. 380-387
    • Receveur, V.1    Calmettes, P.2    Smith, J.C.3    Desmadril, M.4    Coddens, G.5    Durand, D.6
  • 83
    • 0032825667 scopus 로고    scopus 로고
    • Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds
    • REDFIELD, C., SCHULMAN, B. A., MIHOLLEN, M. A., KIM, P. S. & DOBSON, C. M. (1999). Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds. Nature struct. Biol. 6, 948-952.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 948-952
    • Redfield, C.1    Schulman, B.A.2    Mihollen, M.A.3    Kim, P.S.4    Dobson, C.M.5
  • 84
    • 0025877453 scopus 로고
    • Protein hydration and function
    • RUPLEY, J. A. & CARERI, G. (1991). Protein hydration and function. Adv. Protein Chem. 41, 37-172.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 86
    • 0002700870 scopus 로고    scopus 로고
    • Metabolic regulation of selective deuterium incorporation into RNA and protein components of the ribosome
    • eds. S. Cusack, H. Büttner, M. Ferrand, P. Langan & P. Timmins. New York: Adenine Press
    • SCHERBAKOVA, I. V., ZGURSKAYA, E. I., FAN, L. X., SERDYUK, I. N. & ZACCAI, G. (1997). Metabolic regulation of selective deuterium incorporation into RNA and protein components of the ribosome. In Biological Macromolecular Dynamics (eds. S. Cusack, H. Büttner, M. Ferrand, P. Langan & P. Timmins), pp. 165-169. New York: Adenine Press.
    • (1997) Biological Macromolecular Dynamics , pp. 165-169
    • Scherbakova, I.V.1    Zgurskaya, E.I.2    Fan, L.X.3    Serdyuk, I.N.4    Zaccai, G.5
  • 87
    • 0001497571 scopus 로고
    • Electromagnetic neutron-atom interactions
    • SEARS, V. F. (1986). Electromagnetic neutron-atom interactions. Phys. Rep. 5, 281-317.
    • (1986) Phys. Rep. , vol.5 , pp. 281-317
    • Sears, V.F.1
  • 88
    • 0345498055 scopus 로고    scopus 로고
    • Anomalous diffusion of adsorbed water: A neutron scattering study of hydrated myoglobin
    • SETTLES, M. & DOSTER, W. (1996). Anomalous diffusion of adsorbed water: a neutron scattering study of hydrated myoglobin. Faraday Discuss. 103, 269-279.
    • (1996) Faraday Discuss. , vol.103 , pp. 269-279
    • Settles, M.1    Doster, W.2
  • 89
    • 0025938315 scopus 로고
    • Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments
    • SMITH, J. C. (1991). Protein dynamics: comparison of simulations with inelastic neutron scattering experiments. Q. Rev. Biophys. 24, 227-291.
    • (1991) Q. Rev. Biophys. , vol.24 , pp. 227-291
    • Smith, J.C.1
  • 90
    • 0033614354 scopus 로고    scopus 로고
    • The existence of super-cooled liquid water at 150 K
    • SMITH, R. S. & KAY, B. D. (1999). The existence of super-cooled liquid water at 150 K. Nature 398, 788-791.
    • (1999) Nature , vol.398 , pp. 788-791
    • Smith, R.S.1    Kay, B.D.2
  • 91
    • 0033637521 scopus 로고    scopus 로고
    • The dynamics of protein hydration water: A quantitative comparison of molecular dynamics simulations and neutron-scattering experiments
    • TAREK, M. & TOBIAS, D. J. (2000). The dynamics of protein hydration water: a quantitative comparison of molecular dynamics simulations and neutron-scattering experiments. Biophys. 79, 3244-3257.
    • (2000) Biophys. , vol.79 , pp. 3244-3257
    • Tarek, M.1    Tobias, D.J.2
  • 92
    • 0035807881 scopus 로고    scopus 로고
    • Fast dynamics of halophilic malate dehydrogenase and bovine serum albumin measured by neutron scattering under various solvent conditions influencing protein stability
    • TEHEI, M., MADERN, D., PFISTER, C. & ZACCAI, G. (2001). Fast dynamics of halophilic malate dehydrogenase and bovine serum albumin measured by neutron scattering under various solvent conditions influencing protein stability. Proc. natn. Acad. Sci. USA 98, 14356-14361.
    • (2001) Proc. Natn. Acad. Sci. USA , vol.98 , pp. 14356-14361
    • Tehei, M.1    Madern, D.2    Pfister, C.3    Zaccai, G.4
  • 93
    • 0033747018 scopus 로고    scopus 로고
    • Molecular dynamics of solid-state lysozyme as affected by glycerol and water: A neutron scattering study
    • TSAI, A. M., NEUMANN, D. A. & BELL, L. N. (2000). Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study. Biophys. J. 79, 2728-2732.
    • (2000) Biophys. J. , vol.79 , pp. 2728-2732
    • Tsai, A.M.1    Neumann, D.A.2    Bell, L.N.3
  • 94
    • 0034816184 scopus 로고    scopus 로고
    • The inverse relationship between protein dynamics and thermal stability
    • TSAI, A. M., UDOVIC, T. J. & NEUMANN, D. A. (2001). The inverse relationship between protein dynamics and thermal stability. Biophys. J. 81, 2339-2343.
    • (2001) Biophys. J. , vol.81 , pp. 2339-2343
    • Tsai, A.M.1    Udovic, T.J.2    Neumann, D.A.3
  • 95
    • 0000656973 scopus 로고
    • Neutron incoherent scattering law for diffusion in a potential of spherical symmetry: General formalism and application to diffusion inside a sphere
    • VOLINO, F. & DIANOUX, A. J. (1980). Neutron incoherent scattering law for diffusion in a potential of spherical symmetry: general formalism and application to diffusion inside a sphere. Molec. Phys. 41, 271-279.
    • (1980) Molec. Phys. , vol.41 , pp. 271-279
    • Volino, F.1    Dianoux, A.J.2
  • 96
    • 0031990356 scopus 로고    scopus 로고
    • Localization of glycolipids in membranes by in-vivo labelling and neutron diffraction
    • WEIK, M., PATZELT, H., ZACCAI, G. & OESTERHELT, D. (1998). Localization of glycolipids in membranes by in-vivo labelling and neutron diffraction. Molec. Cell 1, 411-419.
    • (1998) Molec. Cell. , vol.1 , pp. 411-419
    • Weik, M.1    Patzelt, H.2    Zaccai, G.3    Oesterhelt, D.4
  • 97
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: R-assessing the protein structure-function paradigm
    • WRIGHT, P. E. & DYSON, H. J. (1999). Intrinsically unstructured proteins: r-assessing the protein structure-function paradigm, J. molec. Biol. 293, 321-331.
    • (1999) J. Molec. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 98
    • 0018356110 scopus 로고
    • Protein-water interactions. Heat capacity of the lysozyme-water system
    • YANG, P. H. & RUPLEY, J. A. (1979). Protein-water interactions. Heat capacity of the lysozyme-water system. Biochemistry 18, 2654-2661.
    • (1979) Biochemistry , vol.18 , pp. 2654-2661
    • Yang, P.H.1    Rupley, J.A.2
  • 99
    • 0038433167 scopus 로고    scopus 로고
    • YELLOW BOOK ILL: http://www.ill.fr/pages/science/IGroups/yb.pdf
    • Yellow Book Ill
  • 100
    • 0023644695 scopus 로고
    • Structure and hydration of purple membranes in different conditions
    • ZACCAI, G. (1987). Structure and hydration of purple membranes in different conditions. J. molec. Biol. 194 (3), 569-572.
    • (1987) J. Molec. Biol. , vol.194 , Issue.3 , pp. 569-572
    • Zaccai, G.1
  • 101
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? A protein force constant measured by neutron scattering
    • ZACCAI, G. (2000a). How soft is a protein? A protein force constant measured by neutron scattering. Science 288, 1604-1607.
    • (2000) Science , vol.288 , pp. 1604-1607
    • Zaccai, G.1
  • 102
    • 0034734280 scopus 로고    scopus 로고
    • Moist and soft, dry and stiff: A review of neutron experiments on hydration-dynamics-activity relations in the purple membrane of Halobacterium salinarum
    • ZACCAI, G. (2000b). Moist and soft, dry and stiff: a review of neutron experiments on hydration-dynamics-activity relations in the purple membrane of Halobacterium salinarum. Biophys. Chem. 86, 249-257.
    • (2000) Biophys. Chem. , vol.86 , pp. 249-257
    • Zaccai, G.1
  • 103
    • 0033683008 scopus 로고    scopus 로고
    • Incoherent elastic neutron scattering as a function of temperature: A fast way to characterise in-situ biological dynamics in complex solutions
    • Pr7-283-287
    • ZACCAI, G., TEHEI, M. SCHERBAKOVA, I., SERDYUK, I., GEREZ, C. & PFISTER, C. (2000). Incoherent elastic neutron scattering as a function of temperature: a fast way to characterise in-situ biological dynamics in complex solutions. Journal de Physique IV 10, Pr7-283-287.
    • (2000) Journal de Physique IV , vol.10
    • Zaccai, G.1    Tehei, M.2    Scherbakova, I.3    Serdyuk, I.4    Gerez, C.5    Pfister, C.6
  • 104
    • 0033028550 scopus 로고    scopus 로고
    • Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: The case of the typical EF-hand calcium-binding parvalbumin
    • ZANOTTI, J. M., BELLISSENT-FUNEL, M. C. & PARELLO, J. (1999). Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin. Biophys. J. 76, 2390-2411.
    • (1999) Biophys. J. , vol.76 , pp. 2390-2411
    • Zanotti, J.M.1    Bellissent-Funel, M.C.2    Parello, J.3


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