Boiling Temperature As a Scaling Parameter for the Microscopic Relaxation Dynamics in Molecular Liquids

At sufficiently high temperatures, the center-of-mass microscopic diffusion dynamics of liquids is characterized by a single component, often with weak temperature dependence. In this regime, the effective cage made by the neighbor particles cannot be sustained and readily breaks down, enabling long-range diffusion. As the temperature is decreased, the cage relaxation becomes impeded, leading to a higher viscosity with more pronounced temperature dependence. On the microscopic scale, the sustained caging effect leads to a separation between a faster in-cage relaxation component and a slower cage-breaking relaxation component. The evidence for the separate dynamic components, as opposed to a single stretched component, is provided by quasielastic neutron scattering experiments. We use a simple method to evaluate the extent of the dynamic components separation as a function of temperature in a group of related aromatic molecular liquids. We find that, regardless of the glass-forming capabilities or lack thereof, progressively more pronounced separation between the in-cage and cage-breaking dynamic components develops on cooling down as the ratio of <i>T</i>_b/<i>T</i>, where <i>T</i>_b is the boiling temperature, increases. This reflects the microscopic mechanism behind the empirical rule for the glass forming capability based on the ratio of boiling and melting temperatures, <i>T</i>_b/<i>T</i>_m. When a liquid’s <i>T</i>_b/<i>T</i>_m happens to be high, the liquid can readily be supercooled below its <i>T</i>_m because the liquid’s microscopic relaxation dynamics is already impeded at <i>T</i>_m, as evidenced by a sustained caging effect manifested through the separation of the in-cage and cage-breaking dynamic components. Our findings suggest certain universality in the temperature dependence of the microscopic diffusion dynamics in molecular liquids, regardless of their glass-forming capabilities. Unless the insufficiently low (with respect to <i>T</i>_b) melting temperature, <i>T</i>_m, intervenes and makes crystallization thermodynamically favorable when cage-breaking is still unimpeded and the structural relaxation is fast, the liquid is likely to become supercooled. The propensity to supercooling and eventually forming a glass is thus determined by a purely thermodynamic factor, <i>T</i>_b/<i>T</i>_m

Differential Microscopic Mobility of Components within a Deep Eutectic Solvent

From macroscopic measurements of deep eutectic solvents such as glyceline (1:2 molar ratio of choline chloride to glycerol), the long-range translational diffusion of the larger cation (choline) is known to be slower compared to that of the smaller hydrogen bond donor (glycerol). However, when the diffusion dynamics are analyzed on the subnanometer length scale, we find that the displacements associated with the localized diffusive motions are actually larger for choline. This counterintuitive diffusive behavior can be understood as follows. The localized diffusive motions confined in the transient cage of neighbor particles, which precede the cage-breaking long-range diffusion jumps, are more spatially constrained for glycerol than for choline because of the stronger hydrogen bonds the former makes with chloride anions. The implications of such differential localized mobility of the constituents should be especially important for applications where deep eutectic solvents are confined on the nanometer length scale and their long-range translational diffusion is strongly inhibited (e.g., within microporous media)

Temperature Dependence of Logarithmic-like Relaxational Dynamics of Hydrated tRNA

The dynamics of RNA within the β-relaxation region of 10 ps to 1 ns is crucial to its biological function. Because of its simpler chemical building blocks and the lack of the side methyl groups, faster relaxational dynamics of RNA compared to proteins can be expected. However, the situation is actually opposite. In this work, the relaxational dynamics of tRNA is measured by quasielastic neutron scattering and analyzed using the mode coupling theory, originally developed for glass-forming liquids. Our results reveal that the dynamics of tRNA follows a log-decay within the β-relaxation region, which is an important trait demonstrated by the dynamics of proteins. The dynamics of hydrated tRNA and lysozyme compared in the time domain further demonstrate that the slower dynamics of tRNA relative to proteins originates from the difference in the folded states of tRNA and proteins, as well as the influence of their hydration water

Mixed Ionic Liquid Improves Electrolyte Dynamics in Supercapacitors

Well-tailored mixtures of distinct ionic liquids can act as optimal electrolytes that extend the operating electrochemical window and improve charge storage density in supercapacitors. Here, we explore two room-temperature ionic liquids, 1-ethyl-3-methylimidazolium bis­(trifluoromethylsulfonyl)­imide (EmimTFSI) and 1-ethyl-3-methylimidazolium tetrafluoroborate (EmimBF₄). We study their electric double-layer behavior in the neat state and as binary mixtures on the external surfaces of onion-like carbon electrodes using quasielastic neutron scattering (QENS) and classical density functional theory techniques. Computational results reveal that a mixture with 4:1 EmimTFSI/EmimBF₄ volume ratio displaces the larger [TFSI^–] anions with smaller [BF₄^–] ions, leading to an excess adsorption of [Emim⁺] cations near the electrode surface. These findings are corroborated by the manifestation of nonuniform ion diffusivity change, complementing the description of structural modifications with changing composition, from QENS measurements. Molecular-level understanding of ion packing near electrodes provides insight for design of ionic liquid formulations that enhance the performance of electrochemical energy storage devices

Quasi-elastic Neutron Scattering Reveals Ligand-Induced Protein Dynamics of a G‑Protein-Coupled Receptor

Light activation of the visual G-protein-coupled receptor (GPCR) rhodopsin leads to significant structural fluctuations of the protein embedded within the membrane yielding the activation of cognate G-protein (transducin), which initiates biological signaling. Here, we report a quasi-elastic neutron scattering study of the activation of rhodopsin as a GPCR prototype. Our results reveal a broadly distributed relaxation of hydrogen atom dynamics of rhodopsin on a picosecond–nanosecond time scale, crucial for protein function, as only observed for globular proteins previously. Interestingly, the results suggest significant differences in the intrinsic protein dynamics of the dark-state rhodopsin versus the ligand-free apoprotein, opsin. These differences can be attributed to the influence of the covalently bound retinal ligand. Furthermore, an idea of the generic free-energy landscape is used to explain the GPCR dynamics of ligand-binding and ligand-free protein conformations, which can be further applied to other GPCR systems

Influence of Surface Oxidation on Ion Dynamics and Capacitance in Porous and Nonporous Carbon Electrodes

We investigate the influence of surface chemistry and ion confinement on capacitance and electrosorption dynamics of room-temperature ionic liquids (RTILs) in supercapacitors. Using air oxidation and vacuum annealing, we produced defunctionalized and oxygen-rich surfaces of carbide-derived carbons (CDCs) and graphene nanoplatelets (GNPs). While oxidized surfaces of porous CDCs improve capacitance and rate handling abilities of ions, defunctionalized nonporous GNPs improve charge storage densities on planar electrodes. Quasi-elastic neutron scattering (QENS) and inelastic neutron scattering (INS) probed the structure, dynamics, and orientation of RTIL ions confined in divergently functionalized pores. Oxidized, ionophilic surfaces draw ions closer to pore surfaces and enhance potential-driven ion transport during electrosorption. Molecular dynamics (MD) simulations corroborated experimental data and demonstrated the significance of surface functional groups on ion orientations, accumulation densities, and capacitance

<i>In Vivo</i> Protein Dynamics on the Nanometer Length Scale and Nanosecond Time Scale

Selectively labeled GroEL protein was produced in living deuterated bacterial cells to enhance its neutron scattering signal above that of the intracellular milieu. Quasi-elastic neutron scattering shows that the in-cell diffusion coefficient of GroEL was (4.7 ± 0.3) × 10^–12 m²/s, a factor of 4 slower than its diffusion coefficient in buffer solution. Internal protein dynamics showed a relaxation time of (65 ± 6) ps, a factor of 2 slower compared to the protein in solution. Comparison to the literature suggests that the effective diffusivity of proteins depends on the length and time scale being probed. Retardation of in-cell diffusion compared to the buffer becomes more significant with the increasing probe length scale, suggesting that intracellular diffusion of biomolecules is nonuniform over the cellular volume. The approach outlined here enables investigation of protein dynamics within living cells to open up new lines of research using “in-cell neutron scattering” to study the dynamics of complex biomolecular systems

Collective Excitations in Protein as a Measure of Balance Between its Softness and Rigidity

In this article, we elucidate the protein activity from the perspective of protein softness and flexibility by studying the collective phonon-like excitations in a globular protein, human serum albumin (HSA), and taking advantage of the state-of-the-art inelastic X-ray scattering (IXS) technique. Such excitations demonstrate that the protein becomes softer upon thermal denaturation due to disruption of weak noncovalent bonds. On the other hand, no significant change in the local excitations is detected in ligand- (drugs) bound HSA compared to the ligand-free HSA. Our results clearly suggest that the protein conformational flexibility and rigidity are balanced by the native protein structure for biological activity

Hydration Control of the Mechanical and Dynamical Properties of Cellulose

The mechanical and dynamical properties of cellulose, the most abundant biomolecule on earth, are essential for its function in plant cell walls and advanced biomaterials. Cellulose is almost always found in a hydrated state, and it is therefore important to understand how hydration influences its dynamics and mechanics. Here, the nanosecond-time scale dynamics of cellulose is characterized using dynamic neutron scattering experiments and molecular dynamics (MD) simulation. The experiments reveal that hydrated samples exhibit a higher average mean-square displacement above ∼240 K. The MD simulation reveals that the fluctuations of the surface hydroxymethyl atoms determine the experimental temperature and hydration dependence. The increase in the conformational disorder of the surface hydroxymethyl groups with temperature follows the cellulose persistence length, suggesting a coupling between structural and mechanical properties of the biopolymer. In the MD simulation, 20% hydrated cellulose is more rigid than the dry form, due to more closely packed cellulose chains and water molecules bridging cellulose monomers with hydrogen bonds. This finding may have implications for understanding the origin of strength and rigidity of secondary plant cell walls. The detailed characterization obtained here describes how hydration-dependent increased fluctuations and hydroxymethyl disorder at the cellulose surface lead to enhancement of the rigidity of this important biomolecule

Enhanced Dynamics of Hydrated tRNA on Nanodiamond Surfaces: A Combined Neutron Scattering and MD Simulation Study

Nontoxic, biocompatible nanodiamonds (ND) have recently been implemented in rational, systematic design of optimal therapeutic use in nanomedicines. However, hydrophilicity of the ND surface strongly influences structure and dynamics of biomolecules that restrict <i>in situ</i> applications of ND. Therefore, fundamental understanding of the impact of hydrophilic ND surface on biomolecules at the molecular level is essential. For tRNA, we observe an enhancement of dynamical behavior in the presence of ND contrary to generally observed slow motion at strongly interacting interfaces. We took advantage of neutron scattering experiments and computer simulations to demonstrate this atypical faster dynamics of tRNA on ND surface. The strong attractive interactions between ND, tRNA, and water give rise to unlike dynamical behavior and structural changes of tRNA in front of ND compared to without ND. Our new findings may provide new design principles for safer, improved drug delivery platforms