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

Jansson, Helén; Swenson, Jan

doi:10.1016/j.bbapap.2009.06.026

Cited by 100 publications

(130 citation statements)

References 38 publications

Supporting

Mentioning

102

Contrasting

Unclassified

Order By: Relevance

“…Changes in the thermal properties of tropomyosin following oxidative modification were determined using a TA Instruments DSC 200 PC for densitometry scanning calorimetry measurements (Jansson & Swenson, 2010). In brief, samples ($15 mg) were heated from 40 to 150°C at a heating rate of 8°C/min and then cooled at the same rate.…”

Section: Densitometry Scanning Calorimetry Analysismentioning

confidence: 99%

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Lin

Yuan

et al. 2016

Food Chemistry

View full text Add to dashboard Cite

Section: Densitometry Scanning Calorimetry Analysismentioning

confidence: 99%

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Lin

Yuan

et al. 2016

Food Chemistry

View full text Add to dashboard Cite

“…The inflection of the elastic intensity at 220 K has a dynamic origin that is compatible with a calorimetric glass transition at 170 K. The temperature dependence of the relaxation times is highly sensitive to data evaluation; it can be brought into perfect agreement with the results of other techniques, without any anomaly. In contrast to bulk water, protein hydration water can be supercooled down to a glass transition at T g ≃ 170 K. Near T g translational degrees of freedom arrest, which induces discontinuities in the specific heat and the thermal expansion coefficient of the hydration water [1][2][3][4]. Due to the dynamic nature of the glass transition, freezing of microscopic degrees of freedom can already be observed far above T g .…”

mentioning

confidence: 99%

“…In contrast to bulk water, protein hydration water can be supercooled down to a glass transition at T g ≃ 170 K. Near T g translational degrees of freedom arrest, which induces discontinuities in the specific heat and the thermal expansion coefficient of the hydration water [1][2][3][4]. Due to the dynamic nature of the glass transition, freezing of microscopic degrees of freedom can already be observed far above T g .…”

mentioning

confidence: 99%

See 1 more Smart Citation

Dynamical Transition of Protein-Hydration Water

et al. 2010

View full text Add to dashboard Cite

Thin layers of water on biomolecular and other nanostructured surfaces can be supercooled to temperatures not accessible with bulk water. Chen et al. [PNAS 103, 9012 (2006)] suggested that anomalies near 220 K observed by quasi-elastic neutron scattering can be explained by a hidden critical point of bulk water. Based on more sensitive measurements of water on perdeuterated phycocyanin, using the new neutron backscattering spectrometer SPHERES, and an improved data analysis, we present results that show no sign of such a fragile-to-strong transition. The inflection of the elastic intensity at 220 K has a dynamic origin that is compatible with a calorimetric glass transition at 170 K. The temperature dependence of the relaxation times is highly sensitive to data evaluation; it can be brought into perfect agreement with the results of other techniques, without any anomaly. In contrast to bulk water, protein hydration water can be supercooled down to a glass transition at T g ≃ 170 K. Near T g translational degrees of freedom arrest, which induces discontinuities in the specific heat and the thermal expansion coefficient of the hydration water [1][2][3][4]. Due to the dynamic nature of the glass transition, freezing of microscopic degrees of freedom can already be observed far above T g .The protein dynamic transition is an abrupt onset of atomic displacements on the microscopic length and time scale probed by quasielastic neutron scattering (QENS). First observed twenty years ago in hydrated myoglobin and lysozyme at T ∆ ≃ 240 K [5], it is now known to be a generic property of hydrated proteins, while it is absent in dehydrated systems. It is therefore related to the dynamics of the hydration shell.In QENS, mean squared dispacements δx 2 are deduced from the elastic scattering intensity S(q, 0). Due to the finite spectrometer resolution (fwhm 2∆ω), one actually measures S(q, |ω| ∆ω). Full spectral measurements show that the anomalous decrease of the central peak is compensated by increasing inelastic wings [5,6]. These effects have been interpreted as precursors of the glass transition. Since QENS probes structural relaxation at ∆ω −1 ≃ 100 ps, while the calorimetric T g refers to a time scale of 100 s, it is natural that T ∆ is located far above T g : the protein dynamic transition is the microscopic manifestation of the glass transition in the hydration shell. The time-scale dependence of T ∆ also explains its variation with viscosity [7][8][9]. * Electronic address: wdoster@ph.tum.de Recently, these views have been challenged by the suggestion that there might be a time-scale independent transition. Support came mainly from QENS experiments on the backscattering spectrometer HFBS at NIST. In hydrated lysozyme, DNA and RNA, a kink was found not only in S(q, |ω| ∆ω), but also in the α relaxation time τ deduced from full spectra S(q, ω) [10][11][12][13]. This change of τ (T ) from high-T super-Arrhenius to low-T Arrhenius behavior at T L ≃ 220 K has been interpreted as a fragile-to-strong-transition (FST) from the...

show abstract

“…Thermal and dynamic studies of globular hydrated proteins revealed the presence of a thermal glass transition in the temperature range from about -110 to -20 o C, depending on the protein, the hydration level and the experimental technique employed [19,[24][25][26][27][28][29][30][31][32]. The origin of the glass transition of globular hydrated proteins is not fully understood and it is believed to be highly connected to water dynamics.…”

Section: ) Introductionmentioning

confidence: 99%

Glass Transition and Water Dynamics in Hyaluronic Acid Hydrogels

et al. 2013

View full text Add to dashboard Cite

, J.; A. Kyritsis; Monleón Pradas, M.; Vallés Lluch, A.; Gallego Ferrer, G.; P. Pissis (2013). Glass transition and water dynamics in hyaluronic acid hydrogels. Food Dielectric measurements contribute to the study of the molecular dynamics of water at biological interfaces, in the case of several biomolecules, such as polysaccharides [14] and hydrated proteins [15][16][17][18][19] and also in the case of synthetic hydrogels [20]. In the case of hydrated proteins, it has been shown that the observed dynamics depends strongly on the hydration level and a minimum amount of water is necessary for the onset of enzymatic activity in globular proteins [21]. The dynamics of water molecules in hydrated proteins which do not form a separate ice phase at subzero temperatures (uncrystallized water), has been extensively studied by dielectric measurements and a main secondary relaxation is recorded, attributed to water molecules in the hydration shell [16,17,19]. The main secondary relaxation of uncrystallized water exhibits similar characteristics in various hosting environments [22,23]. In the case of studies on hydrated proteins at low levels of hydration, the evolution of this main secondary dielectric relaxation of uncrystallized water with is not fully understood and it is believed to be highly connected to water dynamics.Theoretical studies suggest that the glass transition is driven by the translational reorientation of the hydrogen bonded network on the protein surface [33] and also connect the water-protein glass transition to the denaturation of the globular proteins, suggesting that both correspond to energetic sub-states, while an energy criterion for the onset of mobility of strong protein-water bonds is induced [34]. In the case of globular proteins the observed dielectric relaxation associated to the calorimetric glass transition has been attributed in literature to a combined motion of uncrystallized water molecules in the protein hydration shell and segments of the protein surface [19,24,25,30]. Measurements in synthetic hydrogels based on poly(hydroxyl ethyl acrylate) (PHEA) by dielectric and other experimental techniques showed that the segmental α relaxation (dynamic glass transition) is significantly plasticized by water [20]. In addition, correlations were observed between results on the organization of water in the hydrogels and on water effects on polymer dynamics. In particular, distinct changes in the dielectric response at the water content of the completion of the first hydration layer indicated that water molecules themselves contribute to the dielectric response at higher water contents [20]. Despite the extended use of HA hydrogels in biological applications, the dielectric behavior of such materials at low water concentrations and subzero temperatures has not been studied so far in detail. In the existing literature dielectric results refer mainly to dilute aqueous solutions of HA salts and particularly at room temperature, using time-domain dielectric measurements [35]. The present study pr...

show abstract

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

Cited by 100 publications

References 38 publications

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Dynamical Transition of Protein-Hydration Water

Glass Transition and Water Dynamics in Hyaluronic Acid Hydrogels

Contact Info

Product

Resources

About