scholarly journals Salt effects on the picosecond dynamics of lysozyme hydration water investigated by terahertz time-domain spectroscopy and an insight into the Hofmeister series for protein stability and solubility

2016 ◽  
Vol 18 (22) ◽  
pp. 15060-15069 ◽  
Author(s):  
Katsuyoshi Aoki ◽  
Kentaro Shiraki ◽  
Toshiaki Hattori

The addition of salts into protein aqueous solutions causes changes in protein solubility and stability, the ability of which is known to be ordered in the Hofmeister series.

2013 ◽  
Author(s):  
Naoki Yamamoto ◽  
Akané Ishihara ◽  
Azusa Kaneko ◽  
Haruka Iguchi ◽  
Ohki Kambara ◽  
...  

2021 ◽  
Vol 22 (21) ◽  
pp. 11969
Author(s):  
Nikita V. Penkov

Despite more than a century of research on the hydration of biomolecules, the hydration of carbohydrates is insufficiently studied. An approach to studying dynamic hydration shells of carbohydrates in aqueous solutions based on terahertz time-domain spectroscopy assay is developed in the current work. Monosaccharides (glucose, galactose, galacturonic acid) and polysaccharides (dextran, amylopectin, polygalacturonic acid) solutions were studied. The contribution of the dissolved carbohydrates was subtracted from the measured dielectric permittivities of aqueous solutions based on the corresponding effective medium models. The obtained dielectric permittivities of the water phase were used to calculate the parameters describing intermolecular relaxation and oscillatory processes in water. It is established that all of the analyzed carbohydrates lead to the increase of the binding degree of water. Hydration shells of monosaccharides are characterized by elevated numbers of hydrogen bonds and their mean energies compared to undisturbed water, as well as by elevated numbers and the lifetime of free water molecules. The axial orientation of the OH(4) group of sugar facilitates a wider distribution of hydrogen bond energies in hydration shells compared to equatorial orientation. The presence of the carboxylic group affects water structure significantly. The hydration of polysaccharides is less apparent than that of monosaccharides, and it depends on the type of glycosidic bonds.


2020 ◽  
Vol 22 (32) ◽  
pp. 17791-17797 ◽  
Author(s):  
Ligang Chen ◽  
Guanhua Ren ◽  
Liyuan Liu ◽  
Pan Guo ◽  
Endong Wang ◽  
...  

The cooling-induced formation of a hydrate in aqueous NaCl solutions was probed using terahertz time-domain spectroscopy (THz-TDS).


2015 ◽  
Vol 104 (12) ◽  
pp. 4025-4033 ◽  
Author(s):  
Vincent P. Wallace ◽  
Denis Ferachou ◽  
Peng Ke ◽  
Katie Day ◽  
Shahid Uddin ◽  
...  

2017 ◽  
Vol 72 (2) ◽  
pp. 257-267 ◽  
Author(s):  
Nikita Penkov ◽  
Valery Yashin ◽  
Eugeny Fesenko ◽  
Andrew Manokhin ◽  
Eugeny Fesenko

Terahertz time-domain spectroscopy (THz-TDS) was used to determine the spectra (range = 1.2–120 cm−1) of aqueous solutions of bovine serum albumin (BSA) at pH range 2.5–10. Under each of the selected pH, BSA molecules exist in a different conformation, compared to other pH values. The spectra were used to calculate the functions of the dielectric permittivity of BSA solutions. Dielectric functions of the aqueous phase of BSA solutions were calculated based on the Bruggeman model, without the contribution of BSA itself. Fitting of the dielectric functions was performed using a model which includes three water spectral bands: two relaxation bands with relaxation times of about 8.28 and 0.3 ps and a vibrational band with a maximum of about 180 cm−1. The parameters of these bands were determined through fitting and physical interpretation at the molecular level can be provided for each of them. A comparison between the values of model parameters of solutions with BSA and without BSA allowed to conclude that the main effect of BSA is the formation of strongly bound hydration shells in the immediate proximity to the protein molecule. At the same time, the structure of more distant layers of the hydration shells is destroyed, with an increased formation of free water molecules. Some differences are observed in the effect of different BSA conformations on the aqueous phase of solution. The proposed approach can be generalized and applied for studying of a wide class of biological macromolecules in aqueous solutions.


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