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Volumn 118, Issue 11, 2014, Pages 2796-2802

Does a dry protein undergo a glass transition?

Author keywords

[No Author keywords available]

Indexed keywords

GLASS; PROTEINS;

EID: 84897835183     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4104905     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 0024976853 scopus 로고
    • Dynamical Transition of Myoglobin Revealed by Inelastic Neutron Scattering
    • Doster, W.; Cusack, S.; Petry, W. Dynamical Transition of Myoglobin Revealed by Inelastic Neutron Scattering Nature 1989, 337, 754-756
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 3
    • 0141560454 scopus 로고    scopus 로고
    • The 'Glass Transition' in Protein Dynamics: What it is, Why it Occurs, and How to Exploit it
    • Ringe, D.; Petsko, G. A. The 'Glass Transition' in Protein Dynamics: What it is, Why it Occurs, and How to Exploit it Biophys. Chem. 2003, 105, 667-680
    • (2003) Biophys. Chem. , vol.105 , pp. 667-680
    • Ringe, D.1    Petsko, G.A.2
  • 4
    • 0028055167 scopus 로고
    • Calorimetric Studies of the Kinetic Unfreezing of Molecular Motions in Hydrated Lysozyme, Hemoglobin and Myoglobin
    • Sartor, G.; Mayer, E.; Johary, G. P. Calorimetric Studies of the Kinetic Unfreezing of Molecular Motions in Hydrated Lysozyme, Hemoglobin and Myoglobin Biophys. J. 1994, 66, 249-258
    • (1994) Biophys. J. , vol.66 , pp. 249-258
    • Sartor, G.1    Mayer, E.2    Johary, G.P.3
  • 5
    • 0034710450 scopus 로고    scopus 로고
    • Low-Temperature Heat Capacity and Glassy Behaviour of Lysozyme Crystals
    • Miyazaki, Y.; Matsuo, T.; Suga, H. Low-Temperature Heat Capacity and Glassy Behaviour of Lysozyme Crystals J. Phys. Chem. B 2000, 104, 8044-8052
    • (2000) J. Phys. Chem. B , vol.104 , pp. 8044-8052
    • Miyazaki, Y.1    Matsuo, T.2    Suga, H.3
  • 6
    • 71649083072 scopus 로고    scopus 로고
    • The Protein-Solvent Glass Transition
    • Doster, W. The Protein-Solvent Glass Transition Biochim. Biophys. Acta 2010, 1804, 3-14
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 3-14
    • Doster, W.1
  • 7
    • 33646270396 scopus 로고    scopus 로고
    • Low-Temperature Glass Transition of Quenched and Annealed Bovine Serum Albumin Aqueous Solutions
    • Kawai, K.; Suzuki, T.; Oguni, M. Low-Temperature Glass Transition of Quenched and Annealed Bovine Serum Albumin Aqueous Solutions Biophys. J. 2006, 90, 3732-3738
    • (2006) Biophys. J. , vol.90 , pp. 3732-3738
    • Kawai, K.1    Suzuki, T.2    Oguni, M.3
  • 8
    • 84996119529 scopus 로고
    • Low-Temperature Glass Transition in Proteins
    • Morozov, V. N.; Gevorkian, S. G. Low-Temperature Glass Transition in Proteins Biopolymers 1985, 24, 1785-1799
    • (1985) Biopolymers , vol.24 , pp. 1785-1799
    • Morozov, V.N.1    Gevorkian, S.G.2
  • 11
    • 81755184334 scopus 로고    scopus 로고
    • Glass Transition and Dynamics in BSA-Water Mixtures over Wide Ranges of Composition Studied by Thermal and Dielectric Techniques
    • Panagopoulou, A.; Kyritsis, A.; Sabater i Serra, R.; Gomez Ribelles, J. L.; Shinyashiki, N.; Pissis, P. Glass Transition and Dynamics in BSA-Water Mixtures over Wide Ranges of Composition Studied by Thermal and Dielectric Techniques Biochim. Biophys. Acta 2011, 1814, 1984-1996
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1984-1996
    • Panagopoulou, A.1    Kyritsis, A.2    Sabater Serra I, R.3    Gomez Ribelles, J.L.4    Shinyashiki, N.5    Pissis, P.6
  • 12
    • 84859974245 scopus 로고    scopus 로고
    • Protein and Water Dynamics in Bovine Serum Albumin - Water Mixture over Wide Ranges of Composition
    • Panagopoulou, A.; Kyritsis, A.; Shinyashiki, N.; Pissis, P. Protein and Water Dynamics in Bovine Serum Albumin-Water Mixture over Wide Ranges of Composition J. Phys. Chem. B 2012, 116, 4593-4602
    • (2012) J. Phys. Chem. B , vol.116 , pp. 4593-4602
    • Panagopoulou, A.1    Kyritsis, A.2    Shinyashiki, N.3    Pissis, P.4
  • 13
    • 0025877453 scopus 로고
    • Protein Hydration and Function
    • Rupley, J. A.; Careri, G. Protein Hydration and Function Adv. Protein Chem. 1991, 41, 37-172
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 14
    • 0043194670 scopus 로고    scopus 로고
    • Evolution of the Internal Dynamics of Two Globular Proteins from Dry Power to Solution
    • Perez, J.; Zanotti, J.-M.; Durand, D. Evolution of the Internal Dynamics of Two Globular Proteins from Dry Power to Solution Biophys. J. 1999, 77, 454-469
    • (1999) Biophys. J. , vol.77 , pp. 454-469
    • Perez, J.1    Zanotti, J.-M.2    Durand, D.3
  • 16
    • 84881645583 scopus 로고    scopus 로고
    • g in Hydrated Proteins: Trend of Mean Square Displacements after Correcting for the Methyl-Group Rotation Contribution
    • g in Hydrated Proteins: Trend of Mean Square Displacements after Correcting for the Methyl-Group Rotation Contribution J. Chem. Phys. 2013, 138, 235102-1-235102-14
    • (2013) J. Chem. Phys. , vol.138 , pp. 2351021-23510214
    • Ngai, K.L.1    Capaccioli, S.2    Paciaroni, A.3
  • 20
    • 78751568002 scopus 로고    scopus 로고
    • The Two-Step Scenario of the Protein Dynamical Transition
    • Doster, W. The Two-Step Scenario of the Protein Dynamical Transition J. Non-Cryst. Solids 2011, 357, 622-628
    • (2011) J. Non-Cryst. Solids , vol.357 , pp. 622-628
    • Doster, W.1
  • 21
    • 49349114913 scopus 로고    scopus 로고
    • Hydration Water Rotational Motion as a Source of Configurational Entropy Driving Protein Dynamics. Crossovers at 150 and 220 K
    • Zanotti, J.-M.; Gibrat, G.; Bellissent-Funel, M.-C. Hydration Water Rotational Motion as a Source of Configurational Entropy Driving Protein Dynamics. Crossovers at 150 and 220 K Phys. Chem. Chem. Phys. 2008, 10, 4865-4870
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 4865-4870
    • Zanotti, J.-M.1    Gibrat, G.2    Bellissent-Funel, M.-C.3
  • 22
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the Environment on the Protein Dynamical Transition: A Neutron Scattering Study
    • Paciaroni, A.; Cinelli, S.; Onori, G. Effect of the Environment on the Protein Dynamical Transition: a Neutron Scattering Study Biophys. J. 2002, 83, 1157-1164
    • (2002) Biophys. J. , vol.83 , pp. 1157-1164
    • Paciaroni, A.1    Cinelli, S.2    Onori, G.3
  • 23
    • 57049104557 scopus 로고    scopus 로고
    • Influence of Hydration on Protein Dynamics: Combining Dielectric and Neutron Scattering Spectroscopy Data
    • Khadodadi, S.; Pawlus, S.; Sokolov, A. P. Influence of Hydration on Protein Dynamics: Combining Dielectric and Neutron Scattering Spectroscopy Data J. Phys. Chem. B 2008, 112, 14273-14280
    • (2008) J. Phys. Chem. B , vol.112 , pp. 14273-14280
    • Khadodadi, S.1    Pawlus, S.2    Sokolov, A.P.3
  • 24
    • 0030823236 scopus 로고    scopus 로고
    • Picosecond Molecular Motion in Bacteriorhodopsin from Neutron Scattering
    • Fitter, J.; Lechner, R. E.; Dencher, N. A. Picosecond Molecular Motion in Bacteriorhodopsin from Neutron Scattering Biophys. J. 1997, 73, 2126-2137
    • (1997) Biophys. J. , vol.73 , pp. 2126-2137
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 25
    • 0020333863 scopus 로고
    • Protein Dynamics: Mössbauer Spectroscopy on Deoxymyoglobin Crystals
    • Parak, F.; Knapp, E. W.; Kucheida, D. Protein Dynamics: Mössbauer Spectroscopy on Deoxymyoglobin Crystals J. Mol. Biol. 1982, 161, 177-194
    • (1982) J. Mol. Biol. , vol.161 , pp. 177-194
    • Parak, F.1    Knapp, E.W.2    Kucheida, D.3
  • 26
    • 0034595671 scopus 로고    scopus 로고
    • How Soft is a Protein? A Protein Dynamic Force Constant Measured by Neutron Scattering
    • Zaccai, G. How Soft is a Protein? A Protein Dynamic Force Constant Measured by Neutron Scattering Science 2000, 288, 1604-1607
    • (2000) Science , vol.288 , pp. 1604-1607
    • Zaccai, G.1
  • 29
    • 0026720247 scopus 로고
    • Crystalline Ribonuclease A Losses Function below the Dynamical Transition at 220 K
    • Rasmussen, B. F.; Stock, A. M.; Ringe, D.; Petsko, G. A. Crystalline Ribonuclease A Losses Function below the Dynamical Transition at 220 K Nature 1992, 357, 423-424
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 30
    • 0001182665 scopus 로고    scopus 로고
    • Neutron Scattering Evidence of a Boson Peak in Protein Hydration Water
    • Paciaroni, A.; Bizzarri, A. R.; Cannistraro, S. Neutron Scattering Evidence of a Boson Peak in Protein Hydration Water Phys. Rev. E 1999, 60, R2476-R2479
    • (1999) Phys. Rev. e , vol.60
    • Paciaroni, A.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 31
    • 0035339112 scopus 로고    scopus 로고
    • Origin of the Lognormal Shape in the Boson-Peak of Globular Proteins
    • Nöllmann, M.; Etchegoin, P. Origin of the Lognormal Shape in the Boson-Peak of Globular Proteins Physica A 2001, 294, 44-50
    • (2001) Physica A , vol.294 , pp. 44-50
    • Nöllmann, M.1    Etchegoin, P.2
  • 33
    • 0035879037 scopus 로고    scopus 로고
    • Effects of Solvent Damping on Side Chain and Backbone Contributions to the Protein Boson Peak
    • Tarek, M.; Tobias, D. Effects of Solvent Damping on Side Chain and Backbone Contributions to the Protein Boson Peak J. Chem. Phys. 2001, 115, 1607-1612
    • (2001) J. Chem. Phys. , vol.115 , pp. 1607-1612
    • Tarek, M.1    Tobias, D.2
  • 34
    • 20944443949 scopus 로고    scopus 로고
    • Protein Boson Peak Originated from Hydration-Related Multiple Minima Energy Landscape
    • Joti, Y.; Kitao, A.; Go, N. Protein Boson Peak Originated from Hydration-Related Multiple Minima Energy Landscape J. Am. Chem. Soc. 2005, 127, 8705-8709
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8705-8709
    • Joti, Y.1    Kitao, A.2    Go, N.3
  • 35
    • 84888612275 scopus 로고    scopus 로고
    • Stress-Induced Modification of the Boson Peak Scaling Behavior
    • Corezzi, S.; Caponi, S.; Rossi, F.; Fioretto, D. Stress-Induced Modification of the Boson Peak Scaling Behavior J. Phys. Chem. B 2013, 117, 14477-14485
    • (2013) J. Phys. Chem. B , vol.117 , pp. 14477-14485
    • Corezzi, S.1    Caponi, S.2    Rossi, F.3    Fioretto, D.4
  • 36
    • 0028847040 scopus 로고
    • Lyophilization-Induced Reversible Structural Changes in Proteins
    • Grebenow, K.; Klibanov, A. M. Lyophilization-Induced Reversible Structural Changes in Proteins Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 10969-10976
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10969-10976
    • Grebenow, K.1    Klibanov, A.M.2
  • 37
    • 10844239741 scopus 로고    scopus 로고
    • Lysozyme-Water Interactions Studied by Sorption Calorimetry
    • Kocherbitov, V.; Arnebrant, T.; Söderman, O. Lysozyme-Water Interactions Studied by Sorption Calorimetry J. Phys. Chem. B 2004, 108, 19036-19042
    • (2004) J. Phys. Chem. B , vol.108 , pp. 19036-19042
    • Kocherbitov, V.1    Arnebrant, T.2    Söderman, O.3
  • 39
    • 0000781978 scopus 로고
    • Inelastic Neutron Scattering Analysis of Low-Frequency Motions in Proteins: Harmonic and Damped Harmonic Models of Bovine Pancreatic Trypsin Inhibitor
    • Smith, J.; Cusack, S.; Tidor, B.; Karplus, M. Inelastic Neutron Scattering Analysis of Low-Frequency Motions in Proteins: Harmonic and Damped Harmonic Models of Bovine Pancreatic Trypsin Inhibitor J. Chem. Phys. 1990, 93, 2974-2991
    • (1990) J. Chem. Phys. , vol.93 , pp. 2974-2991
    • Smith, J.1    Cusack, S.2    Tidor, B.3    Karplus, M.4
  • 40
    • 0042266782 scopus 로고    scopus 로고
    • Protein Dynamics on the Picosecond Timescale as Affected by the Environment: A Quasielastic Neutron Scattering Study
    • Paciaroni, A.; Orecchini, A.; Cinelli, S.; Onori, G.; Lechner, R. E.; Pieper, J. Protein Dynamics on the Picosecond Timescale as Affected by the Environment: a Quasielastic Neutron Scattering Study Chem. Phys. 2003, 292, 397-404
    • (2003) Chem. Phys. , vol.292 , pp. 397-404
    • Paciaroni, A.1    Orecchini, A.2    Cinelli, S.3    Onori, G.4    Lechner, R.E.5    Pieper, J.6
  • 41
    • 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. Molecular Dynamics of Solid-State Lysozyme as Affected by Glycerol and Water: a Neutron Scattering Study Biophys. J. 2000, 79, 2728-2732
    • (2000) Biophys. J. , vol.79 , pp. 2728-2732
    • Tsai, A.M.1    Neumann, D.A.2    Bell, L.N.3
  • 45
    • 0035942731 scopus 로고    scopus 로고
    • Microscopic Origins of Entropy, Heat Capacity and the Glass Transition in Proteins
    • Lee, A. L.; Wand, J. Microscopic Origins of Entropy, Heat Capacity and the Glass Transition in Proteins Nature 2001, 411, 501-504
    • (2001) Nature , vol.411 , pp. 501-504
    • Lee, A.L.1    Wand, J.2
  • 46
    • 0035826241 scopus 로고    scopus 로고
    • Supercooled Liquids and the Glass Transition
    • Debenedetti, P. G.; Stillinger, F. H. Supercooled Liquids and the Glass Transition Nature 2001, 410, 259-267
    • (2001) Nature , vol.410 , pp. 259-267
    • Debenedetti, P.G.1    Stillinger, F.H.2
  • 47
    • 33750489765 scopus 로고    scopus 로고
    • Slow and Fast Dynamics in Glycerol-Water Mixtures
    • Hayashi, Y.; Puzenko, A.; Feldman, Yu. Slow and Fast Dynamics in Glycerol-Water Mixtures J. Non-Cryst. Solids 2006, 352, 4696-4703
    • (2006) J. Non-Cryst. Solids , vol.352 , pp. 4696
    • Hayashi, Y.1    Puzenko, A.2    Feldman, Yu.3


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