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Volumn 1804, Issue 1, 2010, Pages 20-26

The protein glass transition as measured by dielectric spectroscopy and differential scanning calorimetry

Author keywords

Dielectric spectroscopy; Differential scanning calorimetry; Glass transition; Protein; Protein dynamics; Solvent dynamics

Indexed keywords

GLYCEROL; MYOGLOBIN; SOLVENT; WATER;

EID: 71649095681     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.06.026     Document Type: Article
Times cited : (92)

References (39)
  • 1
    • 0025877453 scopus 로고
    • Protein hydration and function
    • Rupley J.A., and Careri G. Protein hydration and function. Adv. Protein Chem. 41 (1991) 37-172
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 2
    • 0004234024 scopus 로고
    • Rowland S.P. (Ed), American Chemical Society, Washington D.C
    • Rupley J.A., Yang P.H., and Tollin G. In: Rowland S.P. (Ed). Water in Polymers (1980), American Chemical Society, Washington D.C
    • (1980) Water in Polymers
    • Rupley, J.A.1    Yang, P.H.2    Tollin, G.3
  • 3
    • 0027016652 scopus 로고
    • Protein-water interactions determined by dielectric methods
    • Pethig R. Protein-water interactions determined by dielectric methods. Annu. Rev. Phys. Chem. 43 (1992) 177-205
    • (1992) Annu. Rev. Phys. Chem. , vol.43 , pp. 177-205
    • Pethig, R.1
  • 4
    • 25844447310 scopus 로고    scopus 로고
    • Dynamics of water in molecular sieves by dielectric spectroscopy
    • Jansson H., and Swenson J. Dynamics of water in molecular sieves by dielectric spectroscopy. Eur. Phys. J. E 12 (2003) S51-S54
    • (2003) Eur. Phys. J. E , vol.12
    • Jansson, H.1    Swenson, J.2
  • 5
    • 30544445880 scopus 로고    scopus 로고
    • Relation between solvent and protein dynamics as studied by dielectric spectroscopy
    • Jansson H., Bergman R., and Swenson J. Relation between solvent and protein dynamics as studied by dielectric spectroscopy. J. Phys. Chem. B 109 (2005) 24134-24141
    • (2005) J. Phys. Chem. B , vol.109 , pp. 24134-24141
    • Jansson, H.1    Bergman, R.2    Swenson, J.3
  • 6
    • 22944468185 scopus 로고    scopus 로고
    • Dynamics of water in a molecular sieve by quasielastic neutron scattering
    • Swenson J., Jansson H., Howells W.S., and Longeville S. Dynamics of water in a molecular sieve by quasielastic neutron scattering. J. Chem. Phys. 122 (2005) 084505
    • (2005) J. Chem. Phys. , vol.122 , pp. 084505
    • Swenson, J.1    Jansson, H.2    Howells, W.S.3    Longeville, S.4
  • 7
    • 33745408624 scopus 로고    scopus 로고
    • Relaxation processes in supercooled confined water and implications for protein dynamics
    • 247802 1-4
    • Swenson J., Jansson H., and Bergman R. Relaxation processes in supercooled confined water and implications for protein dynamics. Phys. Rev. Lett. 96 (2006) 247802 1-4
    • (2006) Phys. Rev. Lett. , vol.96
    • Swenson, J.1    Jansson, H.2    Bergman, R.3
  • 9
    • 57749091998 scopus 로고    scopus 로고
    • Anomalous behaviour of supercooled water and its implication for protein dynamics
    • Franzese G., and Rubi M. (Eds), Springer-Verlag Berlin, Heidelberger platz 3, D-14197 Berlin, Germany
    • Swenson J., Jansson H., and Bergman R. Anomalous behaviour of supercooled water and its implication for protein dynamics. In: Franzese G., and Rubi M. (Eds). Aspects of Physical Biology: Biological Water, Protein Solutions, Transport and Replication (2008), Springer-Verlag Berlin, Heidelberger platz 3, D-14197 Berlin, Germany 23-42
    • (2008) Aspects of Physical Biology: Biological Water, Protein Solutions, Transport and Replication , pp. 23-42
    • Swenson, J.1    Jansson, H.2    Bergman, R.3
  • 10
    • 57149097454 scopus 로고    scopus 로고
    • Origins of apparent fragile-to-strong transitions of protein hydration waters
    • 225701 1-4
    • Vogel M. Origins of apparent fragile-to-strong transitions of protein hydration waters. Phys. Rev. Lett. 101 (2008) 225701 1-4
    • (2008) Phys. Rev. Lett. , vol.101
    • Vogel, M.1
  • 11
    • 41149101933 scopus 로고    scopus 로고
    • Universal features of water dynamics in solutions of hydrophilic polymers, biopolymers, and small glass-forming materials
    • Cerveny S., Alegria A., and Colmenero J. Universal features of water dynamics in solutions of hydrophilic polymers, biopolymers, and small glass-forming materials. Phys. Rev. E (2008) 77
    • (2008) Phys. Rev. E , pp. 77
    • Cerveny, S.1    Alegria, A.2    Colmenero, J.3
  • 12
    • 43049156446 scopus 로고    scopus 로고
    • The protein "glass" transition and the role of the solvent
    • Ngai K.L., Capaccioli S., and Shinyashiki N. The protein "glass" transition and the role of the solvent. J. Phys. Chem. B 112 (2008) 3826-3832
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3826-3832
    • Ngai, K.L.1    Capaccioli, S.2    Shinyashiki, N.3
  • 13
    • 5144223810 scopus 로고    scopus 로고
    • Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions
    • Fenimore P.W., Frauenfelder H., McMahon B.H., and Young R.D. Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 14408-14413
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14408-14413
    • Fenimore, P.W.1    Frauenfelder, H.2    McMahon, B.H.3    Young, R.D.4
  • 16
    • 11144307257 scopus 로고    scopus 로고
    • Fragile-to-strong liquid transition in deeply supercooled confined water
    • Faraone A., Liu L., Mou C.Y., Yen C.W., and Chen S.H. Fragile-to-strong liquid transition in deeply supercooled confined water. J. Chem. Phys. 121 (2004) 10843-10846
    • (2004) J. Chem. Phys. , vol.121 , pp. 10843-10846
    • Faraone, A.1    Liu, L.2    Mou, C.Y.3    Yen, C.W.4    Chen, S.H.5
  • 17
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 18
    • 0009071257 scopus 로고
    • Formation of glasses from liquids and biopolymers
    • Angell C.A. Formation of glasses from liquids and biopolymers. Science 267 (1995) 1924-1935
    • (1995) Science , vol.267 , pp. 1924-1935
    • Angell, C.A.1
  • 21
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron-scattering
    • Doster W., Cusack S., and Petry W. Dynamical transition of myoglobin revealed by inelastic neutron-scattering. Nature 337 (1989) 754-756
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 22
    • 45449115536 scopus 로고    scopus 로고
    • The dynamical transition of proteins, concepts and misconceptions
    • Doster W. The dynamical transition of proteins, concepts and misconceptions. Eur. Biophys. J. Biophys. Lett. 37 (2008) 591-602
    • (2008) Eur. Biophys. J. Biophys. Lett. , vol.37 , pp. 591-602
    • Doster, W.1
  • 24
    • 55549099943 scopus 로고    scopus 로고
    • Hydration affects both harmonic and anharmonic nature of protein dynamics
    • Nakagawa H., Joti Y., Kitao A., and Kataoka M. Hydration affects both harmonic and anharmonic nature of protein dynamics. Biophys. J. 95 (2008) 2916-2923
    • (2008) Biophys. J. , vol.95 , pp. 2916-2923
    • Nakagawa, H.1    Joti, Y.2    Kitao, A.3    Kataoka, M.4
  • 25
    • 33751392182 scopus 로고
    • Calorimetric glass liquid transition and crystallization behavior of a vitreous, but freezable, water fraction in hydrated methemoglobin
    • Sartor G., Hallbrucker A., Hofer K., and Mayer E. Calorimetric glass liquid transition and crystallization behavior of a vitreous, but freezable, water fraction in hydrated methemoglobin. J. Phys. Chem. 96 (1992) 5133-5138
    • (1992) J. Phys. Chem. , vol.96 , pp. 5133-5138
    • Sartor, G.1    Hallbrucker, A.2    Hofer, K.3    Mayer, E.4
  • 26
    • 0344550545 scopus 로고    scopus 로고
    • The glass transition behavior of the globular protein bovine serum albumin
    • Brownsey G.J., Noel T.R., Parker R., and Ring S.G. The glass transition behavior of the globular protein bovine serum albumin. Biophys. J. 85 (2003) 3943-3950
    • (2003) Biophys. J. , vol.85 , pp. 3943-3950
    • Brownsey, G.J.1    Noel, T.R.2    Parker, R.3    Ring, S.G.4
  • 27
    • 0028055167 scopus 로고
    • Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin, and myoglobin
    • Sartor G., Mayer E., and Johari G.P. Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin, and myoglobin. Biophys. J. 66 (1994) 249-258
    • (1994) Biophys. J. , vol.66 , pp. 249-258
    • Sartor, G.1    Mayer, E.2    Johari, G.P.3
  • 28
    • 0034710450 scopus 로고    scopus 로고
    • Low-temperature heat capacity and glassy behavior of lysozyme crystal
    • Miyazaki Y., Matsuo T., and Suga H. Low-temperature heat capacity and glassy behavior of lysozyme crystal. J. Phys. Chem. B 104 (2000) 8044-8052
    • (2000) J. Phys. Chem. B , vol.104 , pp. 8044-8052
    • Miyazaki, Y.1    Matsuo, T.2    Suga, H.3
  • 29
    • 0022762471 scopus 로고
    • Thermal-properties of water in myoglobin crystals and solutions at subzero temperatures
    • Doster W., Bachleitner A., Dunau R., Hiebl M., and Luscher E. Thermal-properties of water in myoglobin crystals and solutions at subzero temperatures. Biophys. J. 50 (1986) 213-219
    • (1986) Biophys. J. , vol.50 , pp. 213-219
    • Doster, W.1    Bachleitner, A.2    Dunau, R.3    Hiebl, M.4    Luscher, E.5
  • 30
    • 0001071099 scopus 로고
    • Dielectric behavior of adsorbed water. 1. Measurement at room-temperature on TiO2
    • Morimoto T., and Iwaki T. Dielectric behavior of adsorbed water. 1. Measurement at room-temperature on TiO2. J. Chem. Soc., Faraday Trans. I 83 (1987) 943-956
    • (1987) J. Chem. Soc., Faraday Trans. I , vol.83 , pp. 943-956
    • Morimoto, T.1    Iwaki, T.2
  • 31
    • 0029328006 scopus 로고
    • Effect of electrode alterations on the Ac behavior of Li2O-ZnO humidity sensors
    • Costa M.E.V., Mantas P.Q., and Baptista J.L. Effect of electrode alterations on the Ac behavior of Li2O-ZnO humidity sensors. Sens. Actuators, B Chem. 27 (1995) 312-314
    • (1995) Sens. Actuators, B Chem. , vol.27 , pp. 312-314
    • Costa, M.E.V.1    Mantas, P.Q.2    Baptista, J.L.3
  • 32
    • 63949086531 scopus 로고    scopus 로고
    • Insulated electrodes for eliminating conductivity in dielectric relaxation experiments
    • Richert R. Insulated electrodes for eliminating conductivity in dielectric relaxation experiments. Eur. Phys. J. B 68 (2009) 197-200
    • (2009) Eur. Phys. J. B , vol.68 , pp. 197-200
    • Richert, R.1
  • 33
    • 0000980146 scopus 로고    scopus 로고
    • General susceptibility functions for relaxations in disordered systems
    • Bergman R. General susceptibility functions for relaxations in disordered systems. J. Appl. Phys. 88 (2000) 1356-1365
    • (2000) J. Appl. Phys. , vol.88 , pp. 1356-1365
    • Bergman, R.1
  • 34
    • 0031836879 scopus 로고    scopus 로고
    • Real-time observation of conformational fluctuations in Zn-substituted myoglobin by time-resolved transient hole-burning spectroscopy
    • Shibata Y., Kurita A., and Kushida T. Real-time observation of conformational fluctuations in Zn-substituted myoglobin by time-resolved transient hole-burning spectroscopy. Biophys. J. 75 (1998) 521-527
    • (1998) Biophys. J. , vol.75 , pp. 521-527
    • Shibata, Y.1    Kurita, A.2    Kushida, T.3
  • 35
    • 0023645793 scopus 로고
    • Time-domain reflectometry studies of water binding and structural flexibility in chymotrypsin
    • Bone S. Time-domain reflectometry studies of water binding and structural flexibility in chymotrypsin. Biochim. Biophys. Acta 916 (1987) 128-134
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 128-134
    • Bone, S.1
  • 36
    • 66749088613 scopus 로고    scopus 로고
    • Dynamics of a protein and its surrounding environment; a QENS study of myoglobin in water and glycerol mixtures
    • Jansson H., Kargl F., Fernandez-Alonso F., and Swenson J. Dynamics of a protein and its surrounding environment; a QENS study of myoglobin in water and glycerol mixtures. J. Chem. Phys. 130 (2009) 205101-205113
    • (2009) J. Chem. Phys. , vol.130 , pp. 205101-205113
    • Jansson, H.1    Kargl, F.2    Fernandez-Alonso, F.3    Swenson, J.4
  • 38
    • 33750489765 scopus 로고    scopus 로고
    • Slow and fast dynamics in glycerol-water mixtures
    • Hayashi Y., Puzenko A., and Feldman Y. Slow and fast dynamics in glycerol-water mixtures. J. Non-Cryst. Solids 352 (2006) 4696-4703
    • (2006) J. Non-Cryst. Solids , vol.352 , pp. 4696-4703
    • Hayashi, Y.1    Puzenko, A.2    Feldman, Y.3
  • 39
    • 0034688337 scopus 로고    scopus 로고
    • Dynamics of supercooled water in confined geometry
    • Bergman R., and Swenson J. Dynamics of supercooled water in confined geometry. Nature 403 (2000) 283-286
    • (2000) Nature , vol.403 , pp. 283-286
    • Bergman, R.1    Swenson, J.2


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