Fragile-to-strong Dynamic Crossover Research Articles

Erratum to: The fragile-to-strong dynamical crossover and the system viscoelasticity in attractive glass forming colloids

The dynamical arrest phenomena of an adhesive hard-sphere (AHS) colloid, L64-D 2O system has been studied by using calorimetry and the complex shear modulus. This system is characterized by a rich temperature (T) and volume fraction (ϕ) phase diagram with a percolation line (PT). According to the mode-coupling theory (MCT), a cusp-like singularity and two glassy phases, one attractive (AG) and one repulsive (RG), are supposed to coexist in the phase diagram. The MCT scaling laws used to study the shear viscosity with ϕ and T as control parameters propose the existence of fragile-to-strong dynamic crossover (FSDC) analogous to that observed in molecular supercooled liquid glass formers. The measured critical values of the control parameters, coincident with the PT line, where the clustering process generates the AG phase, define the FSDC locus. This is in agreement with the extended mode-coupling theory that takes into account both cage and inter-cluster hopping effects. In this work, we demonstrate, by considering the frequency dependence of the complex moduli, that there is the onset of a system viscoelasticity as an effect of the clustering accompanying the FSDC. We will show as the measured frequency-dependent complex moduli satisfy the scaling relations predicted by the scalar elasticity percolation theory and well account for the system evolution toward the glass transition process.

The fragile-to-strong dynamical crossover and the system viscoelasticity in attractive glass forming colloids

The dynamical arrest phenomena of an adhesive hard-sphere (AHS) colloid, L64-D 2O system has been studied by using calorimetry and the complex shear modulus. This system is characterized by a rich temperature (T) and volume fraction (ϕ) phase diagram with a percolation line (PT). According to the mode-coupling theory (MCT), a cusp-like singularity and two glassy phases, one attractive (AG) and one repulsive (RG), are supposed to coexist in the phase diagram. The MCT scaling laws used to study the shear viscosity with ϕ and T as control parameters propose the existence of fragile-to-strong dynamic crossover (FSDC) analogous to that observed in molecular supercooled liquid glass formers. The measured critical values of the control parameters, coincident with the PT line, where the clustering process generates the AG phase, define the FSDC locus. This is in agreement with the extended mode-coupling theory that takes into account both cage and inter-cluster hopping effects. In this work, we demonstrate, by considering the frequency dependence of the complex moduli, that there is the onset of a system viscoelasticity as an effect of the clustering accompanying the FSDC. We will show as the measured frequency-dependent complex moduli satisfy the scaling relations predicted by the scalar elasticity percolation theory and well account for the system evolution toward the glass transition process.

Dynamics of a globular protein and its hydration water studied by neutron scattering and MD simulations

This review article describes our neutron scattering experiments made in the past four years for the understanding of the single-particle (hydrogen atom) dynamics of a protein and its hydration water and the strong coupling between them. We found that the key to this strong coupling is the existence of a fragile-to-strong dynamic crossover (FSC) phenomenon occurring at around TL = 225±5 K in the hydration water. On lowering of the temperature toward FSC, the structure of hydration water makes a transition from predominantly the high density form (HDL), a more fluid state, to predominantly the low density form (LDL), a less fluid state, derived from the existence of a liquid–liquid critical point at an elevated pressure. We show experimentally that this sudden switch in the mobility of hydration water on Lysozyme, B-DNA and RNA triggers the dynamic transition, at a temperature TD = 220 K, for these biopolymers. In the glassy state, below TD, the biopolymers lose their vital conformational flexibility resulting in a substantial diminishing of their biological functions. We also performed molecular dynamics (MD) simulations on a realistic model of hydrated lysozyme powder, which confirms the existence of the FSC and the hydration level dependence of the FSC temperature. Furthermore, we show a striking feature in the short time relaxation (β-relaxation) of protein dynamics, which is the logarithmic decay spanning 3 decades (from ps to ns). The long time α-relaxation shows instead a diffusive behavior, which supports the liquid-like motions of protein constituents. We then discuss our recent high-resolution X-ray inelastic scattering studies of globular proteins, Lysozyme and Bovine Serum Albumin. We were able to measure the dispersion relations of collective, intra-protein phonon-like excitations in these proteins for the first time. We found that the phonon energies show a marked softening and at the same time their population increases substantially in a certain wave vector range when temperature crosses over the TD. Thus the increase of biological activities above TD has positive correlation with activation of slower and large amplitude collective motions of a protein.

Neutron spin echo measurements of monolayer and capillary condensed water in MCM-41 at low temperatures

Neutron spin echo measurements of monolayer and capillary condensed heavy water (D2O) confined in MCM-41 C10 (pore diameter 2.10 nm) were performed in a temperature range of 190–298 K. The intermediate scattering functions were analyzed by the Kohlrausch–Williams–Watts stretched exponential function. The relaxation times of confined D2O in the capillary condensed state follow remarkably well the Vogel–Fulcher–Tammann equation between 298 and 220 K, whereas below 220 K they show an Arrhenius type behavior. That is, the fragile-to-strong (FTS) dynamic crossover occurs, which has never been seen in experiments on bulk water. On the other hand, for monolayer D2O, the FTS dynamic crossover was not observed in the temperature range measured. The FTS dynamic crossover observed in capillary condensed water would take place in the central region of the pore, not near the pore surface. Because the tetrahedral-like water structure in the central region of the pore is more preserved than that near the pore surface, the FTS dynamic crossover would be concerned with the tetrahedral-like water structure.

Dynamics of a globular protein and its hydration water studied by neutron scattering and MD simulations

This review article describes our neutron scattering experiments made in the past four years for the understanding of the single-particle (hydrogen atom) dynamics of a protein and its hydration water and the strong coupling between them. We found that the key to this strong coupling is the existence of a fragile-to-strong dynamic crossover (FSC) phenomenon occurring at aroundTL= 225±5 K in the hydration water. On lowering of the temperature toward FSC, the structure of hydration water makes a transition from predominantly the high density form (HDL), a more fluid state, to predominantly the low density form (LDL), a less fluid state, derived from the existence of a liquid–liquid critical point at an elevated pressure. We show experimentally that this sudden switch in the mobility of hydration water on Lysozyme, B-DNA and RNA triggers the dynamic transition, at a temperatureTD= 220 K, for these biopolymers. In the glassy state, belowTD, the biopolymers lose their vital conformational flexibility resulting in a substantial diminishing of their biological functions. We also performed molecular dynamics (MD) simulations on a realistic model of hydrated lysozyme powder, which confirms the existence of the FSC and the hydration level dependence of the FSC temperature. Furthermore, we show a striking feature in the short time relaxation (β-relaxation) of protein dynamics, which is the logarithmic decay spanning 3 decades (from ps to ns). The long timeα-relaxation shows instead a diffusive behavior, which supports the liquid-like motions of protein constituents. We then discuss our recent high-resolution X-ray inelastic scattering studies of globular proteins, Lysozyme and Bovine Serum Albumin. We were able to measure the dispersion relations of collective, intra-protein phonon-like excitations in these proteins for the first time. We found that the phonon energies show a marked softening and at the same time their population increases substantially in a certain wave vector range when temperature crosses over theTD. Thus the increase of biological activities aboveTDhas positive correlation with activation of slower and large amplitude collective motions of a protein.

Neutron scattering studies of dynamic crossover phenomena in a coupled system of biopolymer and its hydration water

We have observed a Fragile-to-Strong Dynamic Crossover (FSC) phenomenon of the α-relaxation time and self-diffusion constant in hydration water of three biopolymers: lysozyme, B-DNA and RNA. The mean squared displacement (MSD) of hydrogen atoms is measured by Elastic Neutron Scattering (ENS) experiments. The α-relaxation time is measured by Quasi-Elastic Neutron Scattering (QENS) experiments and the self-diffusion constant by Nuclear Magnetic Resonance (NMR) experiments. We discuss the active role of the FSC of the hydration water in initiating the dynamic crossover phenomenon (so-called glass transition) in the biopolymer. The latter transition controls the flexibility of the biopolymer and sets the low temperature limit of its biofunctionality. Finally, we show an MD simulation of a realistic hydrated powder model of lysozyme and demonstrate the agreement of the MD simulation with the experimental data on the FSC phenomenon in the plot of logarithm of the α-relaxation time vs. 1/T.

Observation of a dynamic crossover in RNA hydration water which triggers a dynamic transition in the biopolymer

High-resolution quasielastic neutron scattering spectroscopy was used to measure H2O and D2O hydrated RNA samples. The contribution of scattering from RNA was subtracted out by taking the difference of the signals between the two samples. The measurements were made at a series of temperatures from 270 K down to 180 K. The relaxing-cage model was used to analyze the difference quasielastic spectra. We observed clear evidence of a fragile-to-strong dynamic crossover (FSC) at TL=220 K in RNA hydration water. We further show that the mean-square displacements of the hydrogen atoms in both RNA and its hydration water exhibit a sharp change in slope at approximately the same temperature 220 K. This latter fact suggests that the dynamic transition in RNA is triggered by the abrupt change of mobility of the hydration water at its FSC temperature.

Observation of a dynamic crossover in water confined in double-wall carbon nanotubes

High-resolution quasielastic neutron scattering spectroscopy was used to measure H2O hydrated double-wall carbon nanotubes (DWNT). The measurements were made at a series of temperatures from 250 K down to 150 K. The relaxing-cage model was used to analyze the quasielastic spectra. We observed clear evidence of a fragile-to-strong dynamic crossover (FSC) at T(L) = 190 K in the confined water. We further show that the mean-square atomic displacement of the hydrogen atoms in water exhibits a sharp change in slope at approximately the same temperature 190 K. Comparing the result with that obtained from the confined water in hydrophilic porous silica material MCM-41, we demonstrate experimentally that water confined in a hydrophobic substrate exhibits a lower dynamic crossover temperature by deltaT(L) approximately = 35 K.

Experimental evidence of fragile-to-strong dynamic crossover in DNA hydration water

We used high-resolution quasielastic neutron scattering spectroscopy to study the single-particle dynamics of water molecules on the surface of hydrated DNA samples. Both H(2)O and D(2)O hydrated samples were measured. The contribution of scattering from DNA is subtracted out by taking the difference of the signals between the two samples. The measurement was made at a series of temperatures from 270 down to 185 K. The relaxing-cage model was used to analyze the quasielastic spectra. This allowed us to extract a Q-independent average translational relaxation time <tau(T)> of water molecules as a function of temperature. We observe clear evidence of a fragile-to-strong dynamic crossover (FSC) at T(L)=222+/-2 K by plotting log<tau(T)> versus T. The coincidence of the dynamic transition temperature T(c) of DNA, signaling the onset of anharmonic molecular motion, and the FSC temperature T(L) of the hydration water suggests that the change of mobility of the hydration water molecules across T(L) drives the dynamic transition in DNA.

Dynamical properties of confined supercooled water: an NMR study

We report a set of dynamical data of confined water measured in avery deeply supercooled regime (290–190 K). Water is contained in silicamatrices (MCM-41-S) which consist of 1D cylindrical pores with diametersd = 14,18 and 24 Å. When confined in these tubular pores, water does not crystallize, andcan be supercooled well below 200 K. We use the NMR technique to obtain thecharacteristic proton relaxation time-constants (the spin–lattice relaxationtime-constant T1 and the spin–spin relaxation time-constant T2) and a directmeasurement of the self-diffusion coefficient in the whole temperature range. Wegive evidence of the existence of a fragile-to-strong dynamic crossover (FSC) atTL = 225 K from the temperature dependence of the self-diffusion coefficient. A combination of theNMR self-diffusion coefficient with the average translational relaxation time, as measured byquasi-elastic neutron scattering, shows a well defined decoupling of transport coefficients, i.e. the breakdown of the Stokes–Einstein relation, on approaching the crossover temperatureTL.

Quasielastic and inelastic neutron scattering investigation of fragile-to-strong crossover indeeply supercooled water confined in nanoporous silica matrices

We investigated, using quasi-elastic and inelastic neutron scattering, the slowsingle-particle dynamics of water confined in laboratory synthesized nanoporous silicamatrices, MCM-41-S, with pore diameters ranging from 10 to 18 Å. Inside the poresof these matrices, the freezing process of water is strongly inhibited down to160 K. We analysed the quasi-elastic part of the neutron scattering spectra with arelaxing-cage model and determined the temperature and pressure dependence of theQ-dependent translational relaxation time and its stretch exponentβ for the time dependence of the self-intermediate scattering function. The calculatedQ-independent average translational relaxation time shows a fragile-to-strong (FS) dynamiccrossover for pressures lower than 1600 bar. Above this pressure, it is no longerpossible to discern the characteristic feature of the FS crossover. Identificationof this end point with the predicted second low-temperature critical point ofwater is discussed. A subsequent inelastic neutron scattering investigation of thelibrational band of water indicates that this FS dynamic crossover is associated with astructural change of the hydrogen-bond cage surrounding a typical water moleculefrom a denser liquid-like configuration to a less-dense ice-like open structure.