Glycerol is a major cryoprotective agent and is widely used to promote protein stabilization. Through a combined experimental and theoretical study, we show that global thermodynamic mixing properties of glycerol...
The remarkable ability of guanidinium chloride (GdmCl) to denature proteins is a well studied yet controversial phenomenon; the exact molecular mechanism is still debatable, especially the role of hydration dynamics, which has been paid less attention. In the present contribution, we have addressed the issue of whether the collective hydrogen bond dynamics of water gets perturbed in the presence of GdmCl and its possible impact on the denaturation of a globular protein human serum albumin (HSA), using terahertz (THz) time domain spectroscopy (TTDS) in the frequency range of 0.3-2.0 THz. The collective hydrogen bond dynamics is determined by fitting the obtained complex dielectric response in a multiple Debye relaxation model. To compare the results, the studies were extended to two more salts: tetramethylguanidinium chloride (TMGdmCl) and sodium chloride (NaCl). It was concluded that the change in hydration dynamics plays a definite role in the protein denaturation process.
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.
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 region (where X is the mole fraction of water in the mixture), whereas in X ∼ 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.
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.
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