37 research outputs found
Dynamics of hydration water in deuterated purple membranes explored by neutron scattering
The function and dynamics of proteins depend on their direct environment, and much evidence has pointed to a strong coupling between water and protein motions. Recently however, neutron scattering measurements on deuterated and natural-abundance purple membrane (PM), hydrated in H2O and D2O, respectively, revealed that membrane and water motions on the ns–ps time scale are not directly coupled below 260 K (Wood et al. in Proc Natl Acad Sci USA 104:18049–18054, 2007). In the initial study, samples with a high level of hydration were measured. Here, we have measured the dynamics of PM and water separately, at a low-hydration level corresponding to the first layer of hydration water only. As in the case of the higher hydration samples previously studied, the dynamics of PM and water display different temperature dependencies, with a transition in the hydration water at 200 K not triggering a transition in the membrane at the same temperature. Furthermore, neutron diffraction experiments were carried out to monitor the lamellar spacing of a flash-cooled deuterated PM stack hydrated in H2O as a function of temperature. At 200 K, a sudden decrease in lamellar spacing indicated the onset of long-range translational water diffusion in the second hydration layer as has already been observed on flash-cooled natural-abundance PM stacks hydrated in D2O (Weik et al. in J Mol Biol 275:632–634, 2005), excluding thus a notable isotope effect. Our results reinforce the notion that membrane-protein dynamics may be less strongly coupled to hydration water motions than the dynamics of soluble proteins
Model for solvent viscosity effect on enzymatic reactions
Why reaction rate constants for enzymatic reactions are typically inversely
proportional to fractional power exponents of solvent viscosity remains to be
already a thirty years old puzzle. Available interpretations of the phenomenon
invoke to either a modification of 1. the conventional Kramers' theory or that
of 2. the Stokes law. We show that there is an alternative interpretation of
the phenomenon at which neither of these modifications is in fact
indispensable. We reconcile 1. and 2. with the experimentally observable
dependence. We assume that an enzyme solution in solvent with or without
cosolvent molecules is an ensemble of samples with different values of the
viscosity for the movement of the system along the reaction coordinate. We
assume that this viscosity consists of the contribution with the weight
from cosolvent molecules and that with the weight from protein matrix and
solvent molecules. We introduce heterogeneity in our system with the help of a
distribution over the weight . We verify the obtained solution of the
integral equation for the unknown function of the distribution by direct
substitution. All parameters of the model are related to experimentally
observable values. General formalism is exemplified by the analysis of
literature experimental data for oxygen escape from hemerythin.Comment: 16 LaTex pages, 5 eps figure
Evidence of coexistence of change of caged dynamics at Tg and the dynamic transition at Td in solvated proteins
Mossbauer spectroscopy and neutron scattering measurements on proteins
embedded in solvents including water and aqueous mixtures have emphasized the
observation of the distinctive temperature dependence of the atomic mean square
displacements, , commonly referred to as the dynamic transition at some
temperature Td. At low temperatures, increases slowly, but it assume
stronger temperature dependence after crossing Td, which depends on the
time/frequency resolution of the spectrometer. Various authors have made
connection of the dynamics of solvated proteins including the dynamic
transition to that of glass-forming substances. Notwithstanding, no connection
is made to the similar change of temperature dependence of obtained by
quasielastic neutron scattering when crossing the glass transition temperature
Tg, generally observed in inorganic, organic and polymeric glass-formers.
Evidences are presented to show that such change of the temperature dependence
of from neutron scattering at Tg is present in hydrated or solvated
proteins, as well as in the solvents used unsurprisingly since the latter is
just another organic glass-formers. The obtained by neutron scattering at
not so low temperatures has contributions from the dissipation of molecules
while caged by the anharmonic intermolecular potential at times before
dissolution of cages by the onset of the Johari-Goldstein beta-relaxation. The
universal change of at Tg of glass-formers had been rationalized by
sensitivity to change in volume and entropy of the beta-relaxation, which is
passed onto the dissipation of the caged molecules and its contribution to
. The same rationalization applies to hydrated and solvated proteins for
the observed change of at Tg.Comment: 28 pages, 10 figures, 1 Tabl
How a Vicinal Layer of Solvent Modulates the Dynamics of Proteins
The dynamics of a folded protein is studied in water and glycerol at a series
of temperatures below and above their respective dynamical transition. The
system is modeled in two distinct states whereby the protein is decoupled from
the bulk solvent at low temperatures, and communicates with it through a
vicinal layer at physiological temperatures. A linear viscoelastic model
elucidates the less-than-expected increase in the relaxation times observed in
the backbone dynamics of the protein. The model further explains the increase
in the flexibility of the protein once the transition takes place and the
differences in the flexibility under the different solvent environments.
Coupling between the vicinal layer and the protein fluctuations is necessary to
interpret these observations. The vicinal layer is postulated to form once a
threshold for the volumetric fluctuations in the protein to accommodate
solvents of different sizes is reached. Compensation of entropic-energetic
contributions from the protein-coupled vicinal layer quantifies the scaling of
the dynamical transition temperatures in various solvents. The protein adapts
different conformational routes for organizing the required coupling to a
specific solvent, which is achieved by adjusting the amount of conformational
jumps in the surface-group dihedrals
Reentrant condensation of lysozyme: Implications for studying dynamics of lysozyme in aqueous solutions of lithium chloride
Temperature dependence of fast fluctuations in single- and double-stranded DNA molecules. A neutron scattering investigation.
International audienceThrough elastic neutron scattering measurements we have investigated the picosecond dynamics of dry and hydrated powders of DNA in the double-stranded (dsDNA) and single-stranded (ssDNA) state, in the wide temperature range from 20 to 300 K. The extracted mean square displacements of DNA hydrogen atoms exhibit an onset of anharmonicity at around 100 K. The dynamics of the hydrated samples shows a further anharmonic contribution appearing at a temperature Td = 230 – 240 K. Such dynamical behaviour is similar to the well-studied dynamical transition found in hydrated protein powders. The mean square displacements of dsDNA and ssDNA are practically superimposed in the whole temperature range for both dry and hydrated samples. This suggests that the DNA local mobility in the picosecond timescale does not depend on the single- or double-stranded conformation
Vibrational density of states measurements in disordered systems
We present a data treatment procedure, based on an iterative technique, properly developed to subtract the multi-phonon contributions from the dynamic structure factor in a self-consistent way. With this technique, we derive the one-phonon vibrational density of states from the dynamic structure factor of different disordered systems, in the framework of the incoherent scattering approximation. We present results on glassy glucose (C6H12O6), a nearly perfect incoherent scatterer, due to high hydrogen content. The data treatment procedure has been found to work well also for the more complex case of dry and hydrated DNA
Temperature-dependent dynamics of water confined in nafion membranes
We performed a neutron scattering study to investigate the dynamical behavior of water absorbed in Nafion at low hydration level as a function of temperature in the range 200-300 K. To single out the spectral contribution of the confined water, the measurements were done on samples hydrated with both H2O and D2O. Due to the strong incoherent scattering cross section of hydrogen atoms with respect to deuterium, in the difference spectra, the contribution from the Nafion membrane is subtracted out and the signal originates essentially from protons in the liquid phase. The main quantities we extracted as a function of the momentum transfer are the elastic incoherent structure factor (EISF) and the line width of the quasielastic component. Their trend suggests that the motion of hydrogen atoms can be schematized as a random jumping inside a confining region, which can be related to the boundaries of the space where water molecules move in the cluster they form around the sulfonic acid site. Through the calculated EISF, we obtained information on the size of such a region, which increases up to 260 K and then attains a constant value. Above this temperature, the number of water protons that are dynamically activated in the accessible time window increases with a faster rate. The jump diffusion dynamics is characterized by a typical jumping time which is stable at 5.3 ps up to similar to 260 K and then gradually decreases. The ensemble of the findings indicates that, within the limits of the energy resolution of the present experiment, water absorbed in the Nafion membrane undergoes a dynamical transition at around 260 K. We discuss the possible relationship of this dynamical onset with the behavior of the electrical conductivity of the membrane as a function of the temperature
Low-frequency dynamics of water absorbed in Nafion membranes as a function of the temperature.
International audienceWe performed a neutron scattering study to investigate the dynamical behavior of water absorbed in Nafion at low hydration level (λ=6, λ = moles of water/moles of sulfonic acid sites) as a function of temperature in the range 200K-300K. To single out the signal of the confined water the measurements were done on samples hydrated with both H2O and D2O in the same temperature range. Due to the strong incoherent scattering cross section of hydrogen atoms with respect to deuterium, in the difference spectra the contribution from the Nafion membrane is subtracted out and most part of the spectra originates from absorbed water. The estimated dynamical susceptibility exhibits features that resemble those of bulk water. In particular, the spectra display a bump at around 1 meV, possibly related to α relaxation, the intensity of which is markedly affected by the temperature change. Two features due to the phonon-like collective hydrogen bond network dynamics are well visible at approximately 7 meV and 25 meV
Dynamics of water confined in fuel cell Nafion membranes containing zirconium phosphate nanofiller
A quasielastic neutron scattering investigation, to study the single particle dynamics of water absorbed in a Nafion/zirconium phosphate composite membrane hydrated at a saturation value, is herewith presented. The measurements were done on samples hydrated with both H2O and D2O to properly select the spectral contribution of the confined water. Both the elastic incoherent structure factor (EISF) and the linewidth of the quasielastic component are evaluated as a function of the momentum transfer. Their trend suggests that the motion of the system hydrogen atoms can be schematized as a random jumping inside a confining spherical region, which can be related to the boundaries of the cluster that water molecules form around the sulfonic and phosphate acid sites. The size of such a region, the characteristic time necessary to explore the region and the number of mobile protons involved in this motion are similar to those estimated for water absorbed in a simple Nafion membrane at a saturation water content. Also the calculated jump diffusion coefficient resembles that of water confined in a simple Nafion membrane, and both are consistent with the value of bulk water. The results indicate that the dynamical behaviour of water in Nafion membranes is nearly unaffected by the presence of zirconium phosphate nanoparticles