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Konstantin K. Turoverov

Researcher at Russian Academy of Sciences

Publications -  181
Citations -  5907

Konstantin K. Turoverov is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Thioflavin & Protein structure. The author has an hindex of 39, co-authored 166 publications receiving 5026 citations. Previous affiliations of Konstantin K. Turoverov include Anschutz Medical Campus & National Academy of Sciences of Belarus.

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What Macromolecular Crowding Can Do to a Protein

TL;DR: The goal of this review is to systematically analyze currently available experimental data on the variety of effects of macromolecular crowding on a protein molecule to represent one of the most comprehensive compendia of the current knowledge in this exciting area.
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Thioflavin T as a molecular rotor: fluorescent properties of thioflavin T in solvents with different viscosity.

TL;DR: The photophysical model successfully explains the fluorescent properties of ThT in solvents with different viscosities and supports the idea that the reason for the characteristic increase in the ThT fluorescence intensity accompanying its incorporation into the amyloid fibrils is determined by the rigidity of the dye environment.
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Spectral Properties of Thioflavin T and Its Complexes with Amyloid Fibrils

TL;DR: In this article, a comparison of the absorption and fluorescence spectra of Thioflavin T (ThT) in various solvents and in the composition of amyloid fibrils has shown that ThT, when excited in the region of the long-wavelength absorption band, fluoresces in the spectral region with a maximum at 478-484 nm.
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Computational study of thioflavin T torsional relaxation in the excited state.

TL;DR: According to the model, a twisted internal charge-transfer (TICT) process takes place for the ThT molecule in the excited singlet state, resulting in a transition from the fluorescent locally excited (LE) state to the nonfluorescent TICT state, accompanied by torsion angle phi growth from 37 to 90 degrees.
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The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation

TL;DR: The functional diversity of these proteins, combined with the variability of signals related to the various intra- and intercellular processes handled by these proteins and their capability to produce multi-variant and multi-directional responses allow them to form a unique regulatory net in a cell.