Catalytic activity, structure and stability of trypsin in an AOT-stabilised water-in-decane microemulsion

Stupishina, E. A.; Faizullin, Dzhigangir A.; Zakharchenko, N. L.; Fedotov, V. D.; Zuev, Yuri F.

doi:10.1070/mc2001v011n06abeh001483

Cited by 10 publications

(2 citation statements)

References 15 publications

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“…Lyophilized ChTr with a molecular weight of 24.8 kDa from bovine pancreas, type II (Sigma-Aldrich) was studied in water solution at T = 25 °C, pH = 3 (adjusted by microliter amounts of HCl), I = 0.01 M NaCl. Protein concentrations were controlled spectrophotometrically using the extinction coefficient E 280 (1%) = 10.01 for α S -CN and E 280 (1%) = 1.36 for ChTr …”

Section: Experimental Sectionmentioning

confidence: 99%

“…Protein concentrations were controlled spectrophotometrically using the extinction coefficient E 280 (1%) = 10.01 for α S -CN 61 and E 280 (1%) = 1.36 for ChTr. 62 The diffusive behaviors of α S -CN and ChTr were analyzed by means of the DLS technique using Photocor Complex (Photocor) equipped with a He−Ne laser (λ = 632.8 nm). The temperature of the cell compartment was controlled within 0.1 °C using a thermoelectric module.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

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Protein Translational Diffusion and Intermolecular Interactions of Globular and Intrinsically Unstructured Proteins

et al. 2019

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The study of intermolecular interactions of proteins has been an important problem for many years. This paper presents an approach to analyze different levels of protein interactions in solutions through a set of the secondand higher-order virial coefficients. The proposed approach is based on the diversified analysis of protein translational collective diffusion and self-diffusion obtained by dynamic light scattering and the pulsed-field gradient NMR (PFG NMR) spectroscopy experimental data. The experimental results were analyzed within the theoretical approach based on Vink's frictional formalism of nonequilibrium thermodynamics and the standard Derjaguin−Landau−Verwey−Overbeekb (DLVO) theory of interactions of colloid particles in electrolyte solutions. The second-and higher-order virial coefficients were obtained to estimate the pairwise and many-body intermolecular interactions in the solutions of globular α-chymotrypsin and intrinsically unstructured α S -casein. The second virial coefficients were calculated from the model of the protein−protein potential of mean force. The description of protein−protein interactions includes a set of interaction potentials: the attractive charge−dipole, dipole−dipole, the dispersion Hamaker, the mean force osmotic-attraction, and the repulsive charge−charge ones. It has been found that the major contribution to the intermolecular α S -casein interactions is made by the repulsive charge−charge potential, whereas for the case of α-chymotrypsin, the contributions from other types of interaction are of importance. It was determined that the model was well suited to describe the interactions of both globular and intrinsically disordered proteins. The suggested combination of Vink's approach and the DLVO theory is novel and holds much promise to make a profound analysis of the processes in systems containing various types of protein molecules.

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Section: Experimental Sectionmentioning

confidence: 99%

Section: ■ Experimental Sectionmentioning

confidence: 99%

Protein Translational Diffusion and Intermolecular Interactions of Globular and Intrinsically Unstructured Proteins

et al. 2019

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Brownian dynamics simulation of substrate motion near active site of enzyme entrapped inside reverse micelle

2010

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Brownian dynamics simulation has been applied to analyze the influence of the electrostatic field of a reverse micelle on the enzyme-substrate complex formation inside a micelle. The probability that the enzyme-substrate complex will form from serine protease (trypsin) and the specific hydrophilic cationic substrate Nalpha-benzoyl-L: -arginine ethyl ester has been studied within the framework of the encounter complex formation theory. It has been shown that surfactant charge, dipole moments created by charged surfactant molecules and counterions, and permittivity of the inner core of reverse micelles can all be used as regulatory parameters to alter the substrate orientation near the active site of the enzyme and to change the probability that the enzyme-substrate complex will form.

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The Effect of Shape and Concentration on Translational Diffusion of Proteins Measured by PFG NMR

et al. 2017

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Catalytic activity, structure and stability of trypsin in an AOT-stabilised water-in-decane microemulsion

Cited by 10 publications

References 15 publications

Protein Translational Diffusion and Intermolecular Interactions of Globular and Intrinsically Unstructured Proteins

Protein Translational Diffusion and Intermolecular Interactions of Globular and Intrinsically Unstructured Proteins

Brownian dynamics simulation of substrate motion near active site of enzyme entrapped inside reverse micelle

The Effect of Shape and Concentration on Translational Diffusion of Proteins Measured by PFG NMR

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