The effect of water dynamics on conformation changes of albumin in pre-denaturation state: photon correlation spectroscopy and simulation

Atamas, N. A.; Bardik, V.Yu.; Банникова, Анна; Grishina, Olga; Lugovskoi, E. V.; Lavoryk, S.; Makogonenko, Yevgen; Korolovych, Volodymyr F.; Nerukh, Dmitry

doi:10.1016/j.molliq.2017.01.017

Cited by 9 publications

(5 citation statements)

References 93 publications

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“…27 At the same time, DLS is used in the study of hydrogenous systems such as polymeric aqueous solutions, alcohols, and homologous disaccharide aqueous solutions. 28,29 In Atamas et al., 30 the DLS method was used in the study of solutions of human serum albumin, the correlation between the conformational dynamics of the protein and the thermal motions in the surrounding water in the physiological temperature range was demonstrated.…”

Section: Resultsmentioning

confidence: 99%

A Study of the Effect of a Protein on the Structure of Water in Solution Using Terahertz Time-Domain Spectroscopy

et al. 2017

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Terahertz time-domain spectroscopy (THz-TDS) was used to determine the spectra (range = 1.2-120 cm) 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. 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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Section: Resultsmentioning

confidence: 99%

A Study of the Effect of a Protein on the Structure of Water in Solution Using Terahertz Time-Domain Spectroscopy

et al. 2017

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“…In recent years, researchers have improved and innovated based on various algorithms in the field of UV-Vis spectrum detection of water quality parameters and established a high-precision prediction model between water quality spectrum data and water quality parameters. These studies have significantly contributed to rapid, accurate detection of water quality parameters [14].…”

Section: Theoretical Basis Of Uv-vis Spectrum Data Processingmentioning

confidence: 99%

Advances on Water Quality Detection by UV-Vis Spectroscopy

et al. 2020

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Water resources are closely linked to human productivity and life. Owing to the deteriorating water resources environment, accurate and rapid determination of the main water quality parameters has become a current research hotspot. Ultraviolet-visible (UV-Vis) spectroscopy offers an effective tool for qualitative analysis and quantitative detection of contaminants in a water environment. In this review, the principle and application of UV-Vis technology in water quality detection were studied. The principle of UV-Vis spectroscopy for detecting water quality parameters and the method of modeling and analysis of spectral data were presented. Various UV-Vis technologies for water quality detection were reviewed according to the types of pollutants, such as chemical oxygen demand, heavy metal ions, nitrate nitrogen, and dissolved organic carbon. Finally, the future development of UV-Vis spectroscopy for the determination of water quality was discussed.

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“…The zeta potential is an important physical parameter that describes the amount of charge present on the protein surface and can be used as an indicator of the protein stability. Temperature is one of the most important factors that affect the ζ of protein (Atamas et al., 2017). Heat treatments led to the decrease of the ζ in CPI, but no significant difference was observed with heating temperature of 65, 75, and 85 ℃ using a protein concentration of 1% (Table 1).…”

Section: Resultsmentioning

confidence: 99%

Effect of heat treatments on the structure and emulsifying properties of protein isolates from cumin seeds (Cuminum cyminum)

Chen

Zhang

et al. 2018

Food sci. technol. int.

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The effect of heat treatments (65, 75, 85, and 95 ℃, 30 min) on the structure and the emulsifying properties of cumin protein isolates were investigated. The fluorescence spectra analysis showed that the conformations were remarkably influenced by heat treatments. An increase in the ratio of α-helix in the secondary structure of heated cumin protein isolates was observed from the result of circular dichroism. Thermal treatments at different temperatures led to an increase in the surface hydrophobicity ( H) and a decrease in zeta potential ( ζ) of cumin protein isolates. Emulsifying activity index and emulsion stability index of heated cumin protein isolates were reduced at different protein concentrations (0.1, 0.5, and 1.0%), while the protein absorption in emulsions stabilized by heated cumin protein isolates gradually increased with heating temperature increasing. Moreover, both emulsions stabilized by native and heated cumin protein isolates showed pseudo-plastic fluid behavior and exhibited a decrease in their viscosities with proteins concentration increasing. But thermal treatments produced different effects on the flow behavior of emulsions formed by various protein concentrations, the flow index for heated cumin protein isolates emulsions increased at protein concentrations of 0.5 and 1.0%, but decreased at a concentration of 0.1%. These results might provide reference for the cumin protein processing and its application in food industry.

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The effect of water dynamics on conformation changes of albumin in pre-denaturation state: photon correlation spectroscopy and simulation

Cited by 9 publications

References 93 publications

A Study of the Effect of a Protein on the Structure of Water in Solution Using Terahertz Time-Domain Spectroscopy

A Study of the Effect of a Protein on the Structure of Water in Solution Using Terahertz Time-Domain Spectroscopy

Advances on Water Quality Detection by UV-Vis Spectroscopy

Effect of heat treatments on the structure and emulsifying properties of protein isolates from cumin seeds (Cuminum cyminum)

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