scholarly journals Solvent Properties of Dichloromethane. IV. Conductivity Studies of Fairly Concentrated Solutions of Tetraalkylammonium-, Tetraphenylarsonium- and Bis(triphenylphosphine)iminium Salts in Dichloromethane.

1985 ◽  
Vol 39b ◽  
pp. 639-655 ◽  
Author(s):  
Idar Svorstøl ◽  
Jon Songstad ◽  
Knut Maartmann-Moe ◽  
Søren Brøgger Christensen ◽  
Gotfryd Kupryszewski ◽  
...  
Keyword(s):  
Concentrated Solutions ◽  
Iminium Salts ◽  
Solvent Properties

scholarly journals The unfolding of iRFP713 in a crowded milieu

2018 ◽  
Author(s):  
Olesya V. Stepanenko ◽  
Olga V Stepanenko ◽  
Irina M. Kuznetsova ◽  
Konstantin K Turoverov
Keyword(s):  
Aqueous Solutions ◽  
Molecular Mass ◽  
Intermediate State ◽  
Excluded Volume ◽  
Concentrated Solutions ◽  
Dextran 40 ◽  
Dextran 70 ◽  
Peg 8000 ◽  
Solvent Properties

The exploring of biological processes in vitro under conditions of macromolecular crowding is a way to achieve an understanding of how these processes occur in vivo. In this work, we study the unfolding of the fluorescent probe iRFP713 in crowded environment in vitro. Previously, we showed that the unfolding of the dimeric iRFP713 is accompanied by the formation of a compact monomer and an intermediate state of the protein. In the intermediate state, the macromolecules of iRFP713 have hydrophobic clusters exposed to the surface of the protein and are prone to aggregation. Concentrated solutions of polyethylene glycol (PEG-8000), Dextran-40 and Dextran-70 with a molecular mass of 8000, 40000 and 70000 Da, respectively, were used to model the conditions for macromolecular crowding. A limited available space provided by all the crowding agents used favors to the enhanced aggregation of iRFP713 in the intermediate state at the concentration of guanidine hydrochloride (GdnHCl), at which the charge of protein surface is neutralized by the guanidine cations. This is in line with the theory of the excluded volume. In concentrated solutions of the crowding agents (240–300 mg/ml), the stabilization of the structure of iRFP713 in the intermediate state is observed. PEG-8000 also enhances the stability of iRFP713 in the monomeric compact state, whereas in concentrated solutions of Dextran-40 and Dextran-70 the resistance of the protein in the monomeric state against GdnHCl-induced unfolding decreases. The obtained data argues for the excluded volume effect being not the only factor that contributes the behavior of biological molecules in a crowded milieu. Crowding agents do not affect the structure of the native dimer of iRFP713, which excludes the direct interactions between the target protein and the crowding agents. PEGs of different molecular mass and Dextran-40/Dextran-70 are known to influence the solvent properties of water. The solvent dipolarity/polarizability and basicity/acidity in aqueous solutions of these crowding agents vary in different ways. The change of the solvent properties in aqueous solutions of crowding agents might impact the functioning of a target protein.

scholarly journals The unfolding of iRFP713 in a crowded milieu

2018 ◽  
Author(s):  
Olesya V. Stepanenko ◽  
Olga V Stepanenko ◽  
Irina M. Kuznetsova ◽  
Konstantin K Turoverov
Keyword(s):  
Aqueous Solutions ◽  
Molecular Mass ◽  
Intermediate State ◽  
Excluded Volume ◽  
Concentrated Solutions ◽  
Dextran 40 ◽  
Dextran 70 ◽  
Peg 8000 ◽  
Solvent Properties

The exploring of biological processes in vitro under conditions of macromolecular crowding is a way to achieve an understanding of how these processes occur in vivo. In this work, we study the unfolding of the fluorescent probe iRFP713 in crowded environment in vitro. Previously, we showed that the unfolding of the dimeric iRFP713 is accompanied by the formation of a compact monomer and an intermediate state of the protein. In the intermediate state, the macromolecules of iRFP713 have hydrophobic clusters exposed to the surface of the protein and are prone to aggregation. Concentrated solutions of polyethylene glycol (PEG-8000), Dextran-40 and Dextran-70 with a molecular mass of 8000, 40000 and 70000 Da, respectively, were used to model the conditions for macromolecular crowding. A limited available space provided by all the crowding agents used favors to the enhanced aggregation of iRFP713 in the intermediate state at the concentration of guanidine hydrochloride (GdnHCl), at which the charge of protein surface is neutralized by the guanidine cations. This is in line with the theory of the excluded volume. In concentrated solutions of the crowding agents (240–300 mg/ml), the stabilization of the structure of iRFP713 in the intermediate state is observed. PEG-8000 also enhances the stability of iRFP713 in the monomeric compact state, whereas in concentrated solutions of Dextran-40 and Dextran-70 the resistance of the protein in the monomeric state against GdnHCl-induced unfolding decreases. The obtained data argues for the excluded volume effect being not the only factor that contributes the behavior of biological molecules in a crowded milieu. Crowding agents do not affect the structure of the native dimer of iRFP713, which excludes the direct interactions between the target protein and the crowding agents. PEGs of different molecular mass and Dextran-40/Dextran-70 are known to influence the solvent properties of water. The solvent dipolarity/polarizability and basicity/acidity in aqueous solutions of these crowding agents vary in different ways. The change of the solvent properties in aqueous solutions of crowding agents might impact the functioning of a target protein.

scholarly journals The unfolding of iRFP713 in a crowded milieu

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e6707
Author(s):  
Olesya V. Stepanenko ◽  
Olga V. Stepanenko ◽  
Irina M. Kuznetsova ◽  
Konstantin K. Turoverov
Keyword(s):  
Aqueous Solutions ◽  
Molecular Mass ◽  
Intermediate State ◽  
Excluded Volume ◽  
Concentrated Solutions ◽  
Dextran 40 ◽  
Dextran 70 ◽  
Peg 8000 ◽  
Solvent Properties

The exploring of biological processes in vitro under conditions of macromolecular crowding is a way to achieve an understanding of how these processes occur in vivo. In this work, we study the unfolding of the fluorescent probe iRFP713 in crowded environment in vitro. Previously, we showed that the unfolding of the dimeric iRFP713 is accompanied by the formation of a compact monomer and an intermediate state of the protein. In the intermediate state, the macromolecules of iRFP713 have hydrophobic clusters exposed to the surface of the protein and are prone to aggregation. Concentrated solutions of polyethylene glycol (PEG-8000), Dextran-40 and Dextran-70 with a molecular mass of 8000, 40000 and 70000 Da, respectively, were used to model the conditions for macromolecular crowding. A limited available space provided by all the crowding agents used favors to the enhanced aggregation of iRFP713 in the intermediate state at the concentration of guanidine hydrochloride (GdnHCl), at which the charge of protein surface is neutralized by the guanidine cations. This is in line with the theory of the excluded volume. In concentrated solutions of the crowding agents (240–300 mg/ml), the stabilization of the structure of iRFP713 in the intermediate state is observed. PEG-8000 also enhances the stability of iRFP713 in the monomeric compact state, whereas in concentrated solutions of Dextran-40 and Dextran-70 the resistance of the protein in the monomeric state against GdnHCl-induced unfolding decreases. The obtained data argues for the excluded volume effect being not the only factor that contributes the behavior of biological molecules in a crowded milieu. Crowding agents do not affect the structure of the native dimer of iRFP713, which excludes the direct interactions between the target protein and the crowding agents. PEGs of different molecular mass and Dextran-40/Dextran-70 are known to influence the solvent properties of water. The solvent dipolarity/polarizability and basicity/acidity in aqueous solutions of these crowding agents vary in different ways. The change of the solvent properties in aqueous solutions of crowding agents might impact the functioning of a target protein.

Molecular Transformations in DNA under the Influence of UV-radiation

2020 ◽  
Vol 04 ◽  
Author(s):  
Vigen G. Barkhudaryan ◽  
Gayane V. Ananyan ◽  
Nelli H. Karapetyan
Keyword(s):  
Uv Radiation ◽  
Uv Irradiation ◽  
Absorption Spectroscopy ◽  
Calf Thymus Dna ◽  
Dilute Solutions ◽  
Concentrated Solutions ◽  
Buffer Solution ◽  
Low Concentration ◽  
Calf Thymus ◽  
Dna Solutions

Background: The processes of destruction and crosslinking of macromolecules occur simultaneously under the influence of ultraviolet (UV) radiation in synthetic polymers, dry DNA and their concentrated solutions. Objective: The effect of UV radiation on calf thymus DNA in dilute solutions subjected to UV- irradiation was studied in this work. Method: The calf thymus DNA was studied in dilute solutions using viscometry, absorption spectroscopy and electrophoresis. Results: It was shown, that at a low concentration of DNA in the buffer solution ([DNA] = 85 μg / ml) under the influence of UV radiation, the processes of destruction of macromolecules and an increase in their flexibility predominate, which is accompanied by a gradual decrease in the viscosity of their solution. In addition, due to the low concentration of the solution, intramolecular crosslinking of macromolecules predominates, which also reduces their size and, consequently, the viscosity of the solution. Conclusion: It was concluded, that in dilute DNA solutions, due to the predominance of the processes of intramolecular crosslinking of macromolecules over intermolecular, only constant processes of decreasing the sizes of DNA macromolecules occur. As a result, its solubility remains virtually unchanged during UV irradiation. The described comments are also excellently confirmed by the results of absorption spectroscopy and electrophoresis

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