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We report the results of THz measurements (30-440 cm -1 ) of aqueous acetic acid solutions over the full mixing range ( X AcAc = 0-1). We recorded spectroscopic observables as a function of the acetic acid concentration in the frequency range of the intermolecular stretch at 150 cm -1 and of the librational modes at 350-440 cm -1 . This allowed us to unravel changes in hydrophobic and hydrophilic hydration motifs, respectively. By means of a novel THz-calorimetry approach, we quantitatively correlated these changes in local hydration motifs to excess mixing entropy and enthalpy. We find that Δ H mix is determined by both hydrophobic and hydrophilic solvation contributions. In contrast, Δ S mix is governed by hydrophobic cavity formation. Our results further suggest that acetic acid-water mixtures are systems at the edge of phase separation due to endothermic contributions from both hydrophilic and hydrophobic solvation in a large portion of the miscibility range. Our work establishes a quantitative relationship between the balance of local hydrophobic and hydrophilic solvation motifs and the macroscopic mixing thermodynamic properties.

The relationship between the local solvation structures and global thermodynamics, specifically in the case of amphiphilic molecules, is a complex phenomenon and is not yet fully understood. With the prior knowledge that local solvation structures can impose a significant impact on the overall solvation process, we here combine THz spectroscopic analysis with MD simulations to investigate the impact of the altered hydrophobicity and polarity of amphiphilic solute molecules on the local solvation configurations. We use two water soluble alcohols: ethanol (EtOH) and its fluorinated counterpart, 2,2,2-trifluoroethanol (TFE), as model solutes. Our study is aimed to determine the relative abundance of different hydrogen bonded conformers and to establish a correlation between the spectral signatures (as obtained from THz spectroscopic measurements) and microscopic solute-solvent interactions associated with the local solvation structures (as obtained from MD simulations). Finally, we estimate the possible energetic parameters associated with the alcohol solubilization process. We found that while both the alcohols are completely water soluble, they receive a contrasting solvation energy share in terms of entropy and enthalpy. We understand that these findings are not limited to the specific system studied here but can be broadly extrapolated to other amphiphilic aqueous solutions.

Glycerol is a major cryoprotective agent and is widely used to promote protein stabilization. By a combined experimental and theoretical study, we show that global thermodynamic mixing properties of glycerol and water are dictated by local solvation motifs. We identify three hydration water populations, i.e. , bulk water, bound water (water hydrogen bonded to the hydrophilic groups of glycerol) and cavity wrap water (water hydrating the hydrophobic moieties). Here, we show that for glycerol experimental observables in the THz regime allow quantification of the abundance of bound water and its partial contribution to the mixing thermodynamics. Specifically, we uncover a 1 : 1 connection between the population of bound waters and the mixing enthalpy, which is further corroborated by the simulation results. Therefore, the changes in global thermodynamic quantity - mixing enthalpy - are rationalized at the molecular level in terms of changes in the local hydrophilic hydration population as a function of glycerol mole fraction in the full miscibility range. This offers opportunities to rationally design polyol water, as well as other aqueous mixtures to optimize technological applications by tuning mixing enthalpy and entropy based on spectroscopic screening., Competing Interests: There are no conflicts to declare., (This journal is © The Royal Society of Chemistry.)

Photo-induced excited-state proton transfer (ESPT) reactions are of central importance in many biological and chemical processes. Identifying mechanistic details of the solvent reorganizations that facilitate proton transfer however, is challenging for current experimental and theoretical approaches. Using optical pump THz probe (OPTP) spectroscopy and molecular dynamics simulations, we were able to elucidate the ultrafast changes in the solvation environment for three derivatives of pyranine: the photoacid HPTS, the methoxy derivative MPTS, and the photobase OPTS. Experimentally, we find damped oscillations in the THz signal at short times and our simulations enable their assignment to vibrational energy transfer beatings between the photoexcited chromophore and nearby solvent molecules. The simulations of HPTS reveal strikingly efficient sub-ps energy transfer into a particular solvent mode, that is active near 4 THz, and which can provide the requisite energy required for solvent reorganization promoting proton transfer. Similar oscillations are present in the THz signal for all three derivatives, however the signal is damped rapidly for HPTS (within 0.4 ps) and more slowly for MPTS (within 1.4 ps) and OPTS (within 2.0 ps). For HPTS, we also characterize an additional phonon-like propagation of the proton into the bulk with a 140 ps period and an 83 ps damping time. Thermalization of the solvent occurs on a time scale exceeding 120 ps., Competing Interests: There are no conflicts to declare., (This journal is © The Royal Society of Chemistry.)

Water, being an active participant in most of the biophysical processes, is important to trace how protein solvation changes as its conformation evolves in the presence of solutes or co-solvents. In this study, we investigate how the secondary structures of two diverse proteins - lysozyme and β-lactoglobulin - change in the aqueous mixtures of two alcohols - ethanol and 2,2,2-trifluoroethanol (TFE) using circular dichroism measurements. We observe that these alcohols change the secondary structures of these proteins and the changes are protein-specific. Subsequently, we measure the collective solvation dynamics of these two proteins both in the absence and in the presence of alcohols by measuring the frequency-dependent absorption coefficient (α(ν)) in the THz (0.1-1.2 THz) frequency domain. The alcohol-water mixtures exhibit a non-ideal behaviour with the highest absorption difference (Δα) obtained at X alcohol = 0.2. The protein solvation in the presence of the alcohols shows an oscillating behaviour in which Δα protein changes with X alcohol . Such an oscillatory behaviour of protein solvation results from a delicate interplay between the protein-water, protein-alcohol and water-alcohol associations. We attempt to correlate the various structural conformations of the proteins with the associated solvation.

It has now been established that large angular jumps do take place when a rotating water molecule exchanges its hydrogen bond (H-bond) identity. This motion differs from the small angular diffusional steps occurring within short time intervals which define the 'Debye diffusion model' of water dynamics. We intend to investigate whether these two processes do eventually complement each other. In this present investigation the orientational dynamics of water in its mixture with a small hydrophobic molecule 1,2-dimethoxy ethane (DME) is studied microscopically using the all-atom classical molecular dynamics (MD) simulation technique. We found that the reorientational motions of water molecules are governed by continuous making and breaking of intermolecular H-bonds with their partners. We characterise these H-bond reorientation motions with the description of the "large amplitude angular jump model" and explore the coupling between the rotational and translational motions. By following the trajectories of each molecule in the solutions we describe the orientational dynamics of liquid water with a 'continuous time random walk' (CTRW) approach. Finally, we explore the diffusivity distribution through the jump properties of the water molecules, which successfully leads to the inherent transient heterogeneity of the solutions. We observe that the heterogeneity increases with increasing DME content in the mixtures. Our study correlates the coupling between rotational and translational motions of water molecules in the mixtures.

Polyethylene glycols (PEGs) can either preferentially bind to biomolecules or exert excluded volume effect depending upon their chain length and concentration. We have studied the effect of ethylene glycol (EG) and PEGs of different chain lengths (M n 400 and 4000) on the enzyme efficiency of hen-egg-white lysozyme (HEWL) on Micrococcus lysodeikticus (M. Lys.) cell. The activity shows a bell-like profile as the turnover number increases from ~1.3 × 10 5  s -1  M -1 in water to ~1.7 × 10 5  s -1  M -1 in presence of 2% PEG-400 beyond which it decreases to ~0.7 × 10 5  s -1  M -1 at 20% PEG-400. Solvent polarity, excluded volume effect, soft nonspecific interactions and structural flexibility are found to be the competing factors which govern the overall enzyme activity as evidenced from circular dichroism (CD) and fluorescence measurements. Thermal unfolding temperature (T m ) of HEWL also shows a bell-shaped profile with PEG concentration which establishes possible correlation with its activity. We also observe a minimum in the activation energy barrier for the catalysis at low osmolyte concentrations. The maximum in the enzyme efficiency has been explained on the basis of an optimization between excluded volume effect and soft interaction among the protein and the cosolutes., (Copyright © 2018 Elsevier B.V. All rights reserved.)

Biological membranes are highly organized supramolecular assemblies of lipids and proteins. The membrane interface separates the outer (bulk) aqueous phase from the hydrophobic membrane interior. In this work, we have explored the microstructure and collective dynamics of the membrane interfacial hydration shell in zwitterionic and negatively charged phospholipid membrane bilayers using terahertz time-domain spectroscopy. We show here that the relaxation time constants of the water hydrogen bond network exhibit a unique "rise and dip" pattern with increasing lipid concentration. More importantly, we observed a dependence of the critical lipid concentration corresponding to the inflection point on the charge of the lipid headgroup, thereby implicating membrane electrostatics as a major factor in the microstructure and dynamics of water at the membrane interface. These results constitute one of the first experimental evidences of the modulation of the dielectric relaxation response of membrane interfacial water by membrane lipid composition in a concentration-dependent manner. Lipid-stringent membrane hydration could be relevant in the broader context of lipid diversity observed in biological membranes and the role of negatively charged lipids in membrane protein structure and function.

Many biologically important processes involve a subtle interplay between Columbic and hydrophobic interactions among molecular groups with water. A comprehensive understanding of such processes, specially while occurring simultaneously in the same molecule is of practical importance. In this contribution, we report the ultrafast (subpicosecond to picosecond) collective hydrogen bond dynamics of water in the extended hydration layers in a series of alkylammonium chloride salts using THz time domain spectroscopic (TTDS) technique (0.3-1.6 THz (10-55 cm -1 )). We found the THz absorption coefficient (α) of the salt solutions systematically vary with the salt type. We obtain the hydrogen bond relaxation dynamics by fitting the frequency dependent dielectric constants in a multiple Debye dielectric relaxation model. We found these salts to transform from being a water "structure breaker" to "structure maker" with increasing carbon content. We also investigate their effect on a model protein "bovine serum albumin" and found a systematic trend toward disrupting the protein secondary structure. The associated changes in the protein hydration in the presence of these salts have also been investigated using TTDS.

We report the experimental observation of nonmonotonic changes in the collective hydration of bovine serum albumin (BSA) in the presence of alcohols of varying carbon-chain lengths, that is, ethanol, 2-propanol, and tert-butyl alcohol (TBA), by using terahertz (THz) time domain spectroscopy. We measured the THz absorption coefficient (α) of the protein solutions, and it was observed that α fluctuated periodically as a function of alcohol concentration at a fixed protein concentration. For a fixed alcohol concentration, an increase in the protein concentration resulted in nonmonotonic changes in α; thus, it first decreased rapidly and then increased, which was followed by a shallow decrease. An alcohol-induced α helix to random coil transition of the protein secondary structure was revealed by circular dichroism spectroscopy measurements, and the effect was most prominent in TBA. The anomalous change in the hydration was found to be a delicate balance between the various interactions present in the three-component system., (© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)

A detailed understanding of hydration of amino acids, the building units of protein, is a key step to realize the overall solvation processes in proteins. In the present contribution, we have made a combined GHz (0.2-50) to THz (0.3-2.0) experimental spectroscopic study to investigate the dynamics of water at room temperature in the presence of different amino acids (glycine, L-serine, L-lysine, L-tryptophan, L-arginine, and L-aspartic acid). The THz absorption coefficient, α(ν), of amino acids follows a trend defined by their solvent accessible surface area. The imaginary and real dielectric constants obtained in GHz and THz regions are fitted into multiple Debye model to obtain various relaxation times. The ∼100 ps time scale obtained in the GHz frequency region is attributed to the rotational motion of the amino acids. In the THz region, we obtain ∼8 ps and ∼200 fs time scales which are related to the cooperative dynamics of H-bond network and partial rotation or sudden jump of the under-coordinated water molecules. These time scales are found to be dependent on the amino acid type and the cooperative motion is found to be dependent on both the hydrophobic as well as the hydrophilic residue of amino acids.

A combined experimental (mid- and far-infrared FTIR spectroscopy and THz time domain spectroscopy (TTDS) (0.3-1.6 THz)) and molecular dynamics (MD) simulation technique are used to understand the evolution of the structure and dynamics of water in its binary mixture with 1,2-dimethoxy ethane (DME) over the entire concentration range. The cooperative hydrogen bond dynamics of water obtained from Debye relaxation of TTDS data reveals a non-monotonous behaviour in which the collective dynamics is much faster in the low X w region (where X w is the mole fraction of water in the mixture), whereas in X w ∼ 0.8 region, the dynamics gets slower than that of pure water. The concentration dependence of the reorientation times of water, calculated from the MD simulations, also captures this non-monotonous character. The MD simulation trajectories reveal presence of large amplitude angular jumps, which dominate the orientational relaxation. We rationalize the non-monotonous, concentration dependent orientational dynamics by identifying two different physical mechanisms which operate at high and low water concentration regimes.

We report the changes in the hydration dynamics around a globular protein, human serum albumin (HSA), in the presence of two short chain crowding agents, namely poly(ethylene glycol)s (PEG 200 and 400). The change in the network water structure is investigated using FTIR spectroscopy in the far-infrared (FIR) frequency range. Site specific changes are obtained by time-resolved fluorescence spectroscopic technique using the intrinsic fluorophore tryptophan (Trp214) of HSA. The collective hydration dynamics of HSA in the presence of PEG molecules are obtained using terahertz (THz) time domain spectroscopy (TTDS) and high intensity p-Ge THz measurements. Our study affirms a considerable perturbation of HSA hydration beyond a critical concentration of PEG.

We report the ultrafast collective hydrogen-bond dynamics of water in the extended hydration layer of urea by using terahertz time-domain spectroscopy in the frequency region of 0.3-2.0 THz. The complex dielectric function has been fitted using a Debye relaxation model, and the timescales obtained are in the order of approximately 9 ps and 200 fs for bulk water; this exhibits a considerable acceleration beyond the 4 M urea concentration and indicates a possible disruption in the collective hydrogen-bonded water-network structure, which, in turn, provides an indirect support for the water "structure-breaking" ability of urea. With 5 M urea in the presence of different concentrations of trimethylamine-N-oxide (TMAO), it was found that these parameters essentially follow the trend observed for TMAO itself, which signifies that any possible disruption of the water structure by urea is outdone by the strong hydrogen-bonding ability of TMAO, which explains its ability to revive urea-denatured proteins to their respective native states., (© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)