A5066706948- thermodynamics and calorimetric analyses
- Analytical Chemistry and Chromatography
- Protein Interaction Studies and Fluorescence Analysis
- Protein purification and stability
- Enzyme Catalysis and Immobilization
- Proteins in Food Systems
- Protein Structure and Dynamics
- Microbial Metabolic Engineering and Bioproduction
- Spectroscopy and Quantum Chemical Studies
- Economic and Technological Developments in Russia
- Agricultural Development and Policies
- Chemical and Physical Properties in Aqueous Solutions
- Chemical Thermodynamics and Molecular Structure
- Crystallization and Solubility Studies
- Thermodynamic properties of mixtures
- Global Trade and Competitiveness
- Enzyme Structure and Function
- Economic Development and Digital Transformation
- Inorganic and Organometallic Chemistry
- Regional Economic Development and Innovation
- Digitalization and Economic Development in Agriculture
- Russia and Soviet political economy
- Photochemistry and Electron Transfer Studies
- Heat shock proteins research
- Chemical Reaction Mechanisms
Kuban State Agrarian University
2024
Krasnodar Research Institute of Storage and Processing of Agricultural Products
2024
Kazan Federal University
2010-2020
This paper considers the scientific grounds of growing complexity economic activity, while indicating sources increasing complexity, means (network organizations, institutions and technologies) that contribute to development in a situation adaptation associated risks.
High precision densitometry was applied to study the hydration of proteins. The process analyzed by simultaneous monitoring excess partial volumes water and proteins in entire range content. Five unrelated (lysozyme, chymotrypsinogen A, ovalbumin, human serum albumin, β-lactoglobulin) were used as models. obtained data compared with enthalpies It shown that quantities are very sensitive changes state At lowest weight fractions (w1), functions can mainly be attributed addition. A transition...
We studied the guanidine hydrochloride (GdnHCl)-, temperature-, and ethanol-induced unfolding of lysozyme using high-precision densitometric measurements, aiming to characterize compare volume changes, Δνo, accompanying a protein simultaneously by different means, that is, GdnHCl, temperature, an organic cosolvent, EtOH. The data obtained are also compared with other means unfolding, such as high-pressure- dimethyl sulfoxide (DMSO)-induced denaturation. To aid in interpreting temperature...
The aim of this study is to simultaneously monitor the excess partial Gibbs energies, enthalpies, and entropies water white egg lysozyme demonstrate how these quantities correlate with coverage protein macromolecules by molecules. Isothermal calorimetry sorption measurements were applied characterize hydration dependencies thermodynamic functions. are found be sensitive changes in states. At lowest weight fractions (w1), functions primarily attributable addition water. transition from a...
Isothermal batch calorimetry was applied to study the hydration of proteins. The process analyzed by simultaneous monitoring excess partial enthalpies water and proteins in entire range content. Four unrelated (lysozyme, chymotrypsinogen A, human serum albumin, β-lactoglobulin) were used as models. quantities are very sensitive changes state At lowest weight fractions (w(1)), thermochemical functions can mainly be attributed addition. A transition from glassy flexible is accompanied...
Human heat shock protein 90 (Hsp90) is a key player in the homeostasis of proteome and plays role numerous diseases, such as cancer. For design Hsp90 ATPase activity inhibitors, it important to understand relationship between an inhibitor structure its inhibition potential. The volume binding one most parameters that are rarely being studied. Here, volumes several ligands recombinant were obtained by three independent experimental techniques: fluorescent pressure shift assay, vibrating tube...
The aim of our study is to monitor the preferential hydration/solvation protein macromolecules at low and high water content in water-organic mixtures. Our approach based on analysis absolute values water/organic solvent sorption. We applied this estimate stabilization/destabilization due interactions α-chymotrypsin with water-acetonitrile At content, preferentially hydrated. intermediate interaction changed from hydration binding acetonitrile. From infrared spectra, changes structure were...
Preferential solvation/hydration is an effective way for regulating the mechanism of protein destabilization/stabilization. Organic solvent/water sorption and residual enzyme activity measurements were performed to monitor preferential hen egg-white lysozyme at high low water content in acetonitrile 25 °C. The obtained results show that destabilization/stabilization depends essentially on initial hydration level acetonitrile. There are three composition regimes dried lysozyme. At content,...
Abstract A thermochemical model for describing the transfer of water from protein phase to organic solvent liquid and determining how solvation ability solvents affects this process was developed. Enthalpy changes on interaction dried hydrated human serum albumin (HSA) with hydrophilic (dimethyl sulfoxide, formamide, ethanol, methanol acetic acid) were measured by isothermal calorimetry at 25 °C. The initial hydration level varied in entire content range 0–30 % [g water/g HSA]. dependence...
Abstract The dependence of the amount water bound to human serum albumin (HSA) suspended in water–dioxane mixtures vs equilibrium concentration liquid phase was determined by Fisher method at 298 K. Langmuir model used order describe isotherm sorption HSA low concentrations solvent. calculated constant adsorption (3.8 ± 0.6 l mol −1 ) is good agreement with obtained earlier from calorimetric data. comparison reported enthalpies suspension formation showed that solvent, only process...