Vitrification effects in water—protein systems

Barkalov, I.M.; Bol’shakov, A. I.; Goldanskii, V. I.; Krupyanskiǐ, Yu. F.

doi:10.1016/0009-2614(93)80066-x

Cited by 9 publications

(10 citation statements)

References 12 publications

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“…The temperature range of the jump shifted toward the higher temperatures by a few tens of Kelvin. These observations were also consistent with those reported by other researchers (20)(21)(22)25,27).…”

Section: Heat Capacities Of the Quenched And Annealed Samplessupporting

confidence: 93%

“…The glass transition of proteins has been demonstrated through a change in the temperature dependence of the mean-square displacement of the atoms using Mössbauer spectroscopy (4), neutron scattering (5)(6)(7), and x-ray scattering (3,8). Infrared spectroscopic (9)(10)(11)(12)(13)(14)(15)(16)(17)(18), dielectric (19), and calorimetric (9,(20)(21)(22)(23)(24)(25)(26)(27) approaches have also been applied to examine the glass transition. Based on these experimental observations, the glass transition of a hydrated protein is thought to depend strongly on the dynamic property of the solvent and occurs over a wide temperature range as a result of the wide distribution in the structural relaxation times of molecules.…”

Section: Introductionmentioning

confidence: 99%

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Low-Temperature Glass Transitions of Quenched and Annealed Bovine Serum Albumin Aqueous Solutions

Kawai

Suzuki

Oguni

2006

Biophysical Journal

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To investigate the glass transition behaviors of a 20% (w/w) aqueous solution of bovine serum albumin, heat capacities and enthalpy relaxation rates were measured by adiabatic calorimetry at temperatures ranging from 80 to 300 K. One series of measurements was carried out after quenching from 300 down to 80 K and another after annealing in 200-240 K. The quenched sample showed a heat capacity jump indicating a glass transition temperature T(g) = 170 K, and the annealed sample showed a smaller jump with the T(g) shifted toward the higher temperature side. The temperature dependence of the enthalpy relaxation rates for the quenched sample indicated the presence of two enthalpy relaxation effects: one at around 110 K and the other over a wide temperature range (120-190 K). The annealed sample showed three separate relaxation effects giving 1) T(g) = 110 K, 2) 135 K, and 3) temperature higher than 180 K, whereas nothing around 170 K. These effects were thought to originate, respectively, from the rearrangement motions of 1) primary hydrate water forming a direct hydrogen bond with the protein, 2) part of the internal water localized in the opening of a protein structure, and 3) the disordered region in the protein.

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Section: Heat Capacities Of the Quenched And Annealed Samplessupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Low-Temperature Glass Transitions of Quenched and Annealed Bovine Serum Albumin Aqueous Solutions

Kawai

Suzuki

Oguni

2006

Biophysical Journal

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“…Other calorimetric studies of water-protein systems for similar hydration range have been reported and we mention only a few of these by, e.g., Mrevlishvili (1979), Doster et al (1986), Goldanskii and Krupyanskii (1989), Barkalov et al (1993), and Czybulka et al (1993). In these studies the calorimetric features of the vitreous, but freezable, water fraction have not been characterized in the same manner as in this work.…”

Section: Introductionmentioning

confidence: 91%

Characterizing the secondary hydration shell on hydrated myoglobin, hemoglobin, and lysozyme powders by its vitrification behavior on cooling and its calorimetric glass-->liquid transition and crystallization behavior on reheating

Sartor

Hallbrucker

Mayer

1995

Biophysical Journal

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For hydrated metmyoglobin, methemoglobin, and lysozyme powders, the freezable water fraction of between approximately 0.3-0.4 g water/g protein up to approximately 0.7-0.8 g water/g protein has been fully vitrified by cooling at rates up to approximately 1500 K min-1 and the influence of cooling rate characterized by x-ray diffractograms. This vitreous but freezable water fraction started to crystallize at approximately 210 K to cubic ice and at approximately 240 K to hexagonal ice. Measurements by differential scanning calorimetry have shown that this vitreous but freezable water fraction undergoes, on reheating at a rate of 30 K min-1, a glass-->liquid transition with an onset temperature of between approximately 164 and approximately 174 K, with a width of between approximately 9 and approximately 16 degrees and an increase in heat capacity of between approximately 20 and approximately 40 J K-1 (mol of freezable water)-1 but that the glass transition disappears upon crystallization of the freezable water. These calorimetric features are similar to those of water imbibed in the pores of a synthetic hydrogel but very different from those of glassy bulk water. The difference to glassy bulk water's properties is attributed to hydrophilic interaction and H-bonding of the macromolecules' segments with the freezable water fraction, which thereby becomes dynamically modified. Abrupt increase in minimal or critical cooling rate necessary for complete vitrification is observed at approximately 0.7-0.8 g water/g protein, which is attributed to an abrupt increase of water's mobility, and it is remarkably close to the threshold value of water's mobility on a hydrated protein reported by Kimmich et al. (1990, Biophys. J. 58:1183). The hydration level of approximately 0.7-0.8 g water/g protein is approximately that necessary for completing the secondary hydration shell.

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“…Additional disorder may result from relaxation of protein conformation (Young et al, 1991) and from differential expansion of the protein lattice and solvent (Juers & Matthews, 2001; Kriminski et al, 2002). Rapid or¯a sh' cooling a crystal to below water's glass transition at T g 9 140 K can freeze water into an amorphous (vitreous) form (Barkalov et al, 1993; and prevent its redistribution within the crystal and generally yields the best diffraction results.…”

Section: Introductionmentioning

confidence: 99%

Heat transfer from protein crystals: implications for flash-cooling and X-ray beam heating

Kriminski

Kazmierczak

Thorne

2003

Acta Crystallogr D Biol Crystallogr

143

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Three problems involving heat transfer from a protein crystal to a cooling agent are analyzed: flash-cooling in a cold nitrogen- or helium-gas stream, plunge-cooling into liquid nitrogen, propane or ethane and crystal heating in a cold gas stream owing to X-ray absorption. Heat transfer occurs by conduction inside the crystal and by convection from the crystal's outer surface to the cooling fluid. For flash-cooling in cold gas streams, heat transfer is limited by the rate of external convection; internal temperature gradients and crystal strains during cooling are very small. Helium gas provides only a threefold improvement in cooling rates relative to nitrogen because its much larger thermal conductivity is offset by its larger kinematic viscosity. Characteristic cooling times vary with crystal size L as L(3/2) and theoretical estimates of these times are consistent with experiments. Plunge-cooling into liquid cryogens, which can give much smaller convective thermal resistances provided that surface boiling is eliminated, can increase cooling rates by more than an order of magnitude. However, the internal conduction resistance is no longer negligible, producing much larger internal temperature gradients and strains that may damage larger crystals. Based on this analysis, factors affecting the success of flash-cooling experiments can be ordered from most to least important as follows: (1) crystal solvent content and solvent composition, (2) crystal size and shape, (3) amount of residual liquid around the crystal, (4) cooling method (liquid plunge versus gas stream), (5) choice of gas/liquid and (6) relative speed between cooling fluid and crystal. Crystal heating by X-ray absorption on present high-flux beamlines should be small. For a fixed flux and illuminated area, heating can be reduced by using crystals with areas normal to the beam that are much larger than the beam area.

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Vitrification effects in water—protein systems

Cited by 9 publications

References 12 publications

Low-Temperature Glass Transitions of Quenched and Annealed Bovine Serum Albumin Aqueous Solutions

Low-Temperature Glass Transitions of Quenched and Annealed Bovine Serum Albumin Aqueous Solutions

Characterizing the secondary hydration shell on hydrated myoglobin, hemoglobin, and lysozyme powders by its vitrification behavior on cooling and its calorimetric glass-->liquid transition and crystallization behavior on reheating

Heat transfer from protein crystals: implications for flash-cooling and X-ray beam heating

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