Publications by authors named "Kirill V Kovalev"
Article Synopsis
- Destabilase is an enzyme from the medical leech that can break down bacterial cell walls and dissolve blood clots.
- It is affected by sodium chloride, which stops its ability to work, but the reason for this wasn't clear until now.
- Researchers discovered the structure of destabilase and think that a different part of the enzyme helps it break down blood clots instead of what was thought before; this could help design new medicines.
Despite remarkable progress, mainly due to the development of LCP and 'bicelle' crystallization, lack of structural information remains a bottleneck in membrane protein (MP) research. A major reason is the absence of complete understanding of the mechanism of crystallization. Here we present small-angle scattering studies of the evolution of the "bicelle" crystallization matrix in the course of MP crystal growth.
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- The study investigates the functional properties of light-sensitive proteins, bacteriorhodopsin (bR) and channelrhodopsin 2 (ChR2), using planar bilayer lipid membranes (BLMs) to measure electric currents.
- The photocurrents exhibited different behaviors depending on the protein: bR showed unidirectional current flow regardless of voltage polarity, while ChR2's current increased with voltage and reversed direction with polarity changes.
- The efficiency of protonophore treatments, specifically TTFB and CCCP, differed significantly, affecting the photocurrents, with TTFB enhancing stationary photocurrents and CCCP reducing them significantly for both proteins.