Coincidence of Dynamical Transitions in a Soluble Protein and Its Hydration Water:  Direct Measurements by Neutron Scattering and MD Simulations

Wood, Kathleen; Frölich, Andreas; Paciaroni, Alessandro; Moulin, Martine; Härtlein, Michael; Zaccaı̈, Giuseppe; Tobias, Douglas J.; Weik, Martin H.

doi:10.1021/ja710526r

Cited by 193 publications

(277 citation statements)

References 27 publications

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“…The deuterated MBP in H 2 O gave access to the dynamics of hydration water, which contributes 73% to the total incoherent scattering cross section but only 2% in natural abundance MBP in D 2 O. The MSD of water and protein motions, plotted in Figure 1A, are similar up to 220 K, at which temperature they both exhibit a transition 27 .…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, however, the onset of hydration water translational diffusion at 200 K, in a membrane, was not observed to trigger a dynamical transition in the membrane protein 25,26 , suggesting a more complex interaction between protein, water, and the membrane lipid environment. Recent neutron scattering studies, using specific deuterium labelling, confirmed that a dynamical transition coincides with the onset of hydration water translational diffusion, in the case of a soluble proteins 27 , but not in the case of a membrane protein 3,28 .…”

Section: Introductionmentioning

confidence: 99%

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From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity

et al. 2009

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An integrated picture of hydration shell dynamics and of its coupling to functional macromolecular motions is proposed from studies on a soluble protein, on a membrane protein in its natural lipid environment, and on the intracellular environment in bacteria and red blood cells. Water dynamics in multimolar salt solutions was also examined, in the context of the very slow water component previously discovered in the cytoplasm of extreme halophilic archaea. The data were obtained from neutron scattering by using deuterium labelling to focus on the dynamics of different parts of the complex systems examined.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity

et al. 2009

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“…The change in slope of the temperature dependence of hydrated protein's mean-square displacement around 220 K has been extensively studied, 9,11,13,23,24,67,68 as this transition is connected to protein function and vanishes in the absence of hydration. It has been proposed that the dynamical crossover around 220 K could be associated with a large scale structural change in hydrogen bond connectivity.…”

Section: Discussionmentioning

confidence: 99%

“…The steeper increase above 220-230 K is usually correlated with the so called dynamic transition, reflecting the increase in internal rotation and translation dynamics. 9,12,13,23,24,28,32 The hu 2 i values for a nominally dry sample (Fig. 1, inset) shows linear temperature dependence up to about 240 K, and a deviation from linearity above this temperature.…”

Section: Neutron Scatteringmentioning

confidence: 95%

Hydration water and peptide dynamics – two sides of a coin. A neutron scattering and adiabatic calorimetry study at low hydration and cryogenic temperatures

Bastos

Alves

Maia

et al. 2013

Phys. Chem. Chem. Phys.

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In the present work we bridge neutron scattering and calorimetry in the study of a low-hydration sample of a 15-residue hybrid peptide from cecropin and mellitin CA(1-7)M(2-9) of proven antimicrobial activity.Quasielastic and low-frequency inelastic neutron spectra were measured at defined hydration levelsa nominally 'dry' sample (specific residual hydration h = 0.060 g/g), a H 2 O-hydrated (h = 0.49) and a D 2 Ohydrated one (h = 0.51). Averaged mean square proton mobilities were derived over a large temperature range (50-300 K) and the vibrational density of states (VDOS) were evaluated for the hydrated samples. The heat capacity of the H 2 O-hydrated CA(1-7)M(2-9) peptide was measured by adiabatic calorimetry in the temperature range 5-300 K, for different hydration levels. The glass transition and water crystallization temperatures were derived in each case. The existence of different types of water was inferred and their amounts calculated. The heat capacities as obtained from direct calorimetric measurements were compared to the values derived from the neutron spectroscopy by way of integrating appropriately normalized VDOS functions. While there is remarkable agreement with respect to both temperature dependence and glass transition temperatures, the results also show that the VDOS derived part represents only a fraction of the total heat capacity obtained from calorimetry. Finally our results indicate that both hydration water and the peptide are involved in the experimentally observed transitions.

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“…These motions actually involve the atoms not just of the biological structure itself but also of the surrounding medium with which a coupling exists. Therefore, depending on the circumstances, the protein can be considered "slaved" or "sequestered" by the host medium which can be able to suppress its dynamics, so resulting in a retardation of denaturation processes or a slowing down of biological function [4][5][6][7][8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Study of solvent–protein coupling effects by neutron scattering

et al. 2009

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The present work aims to characterize the dynamical behavior of proteins immersed in bio-preserving liquids and glasses. For this purpose, the protein dUTPase was chosen, while the selected solvents were glycerol, a triol, and some homologous disaccharides, i.e., trehalose, maltose, and sucrose, which are known to be very effective bio-preserving agents. The results highlight that the disaccharides show a slowing down effect on the water dynamics, which is stronger for trehalose than in the case of the other disaccharides. Furthermore, a characterization of the medium which hosts the protein is performed by using an operative definition of fragility based on the mean square displacement extracted by elastic incoherent neutron scattering, which is directly connected to Angell's kinetic fragility based on the viscosity. Finally, a study of the dynamics of the protein sequestered within the solvents is performed. The result shows that the protein dynamics is coupled with that of the surrounding matrix.

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Coincidence of Dynamical Transitions in a Soluble Protein and Its Hydration Water: Direct Measurements by Neutron Scattering and MD Simulations

Cited by 193 publications

References 27 publications

From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity

From shell to cell: neutron scattering studies of biological water dynamics and coupling to activity

Hydration water and peptide dynamics – two sides of a coin. A neutron scattering and adiabatic calorimetry study at low hydration and cryogenic temperatures

Study of solvent–protein coupling effects by neutron scattering

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