Articles tagged with Conformational Change
Researchers at the University of Osaka developed flexible molecules with movable segments that efficiently emit orange-to-red light, bypassing the need for rigid structures. The new molecules have an S shape and can adopt various conformations, allowing for high-performance OLEDs with a relatively high level of performance
Scientists at The University of Osaka have created a multipath synergistic strategy to toughen elastomers by sequentially activating three energy dissipation pathways. This approach enhances the material's toughness while maintaining its elasticity, making it suitable for various applications such as tires, gloves, and adhesives.
A team of researchers from China and the UK has developed new ways to optimise the production of solar fuels by creating novel photocatalysts. These photocatalysts, such as titanium dioxide with boron nitride, can absorb more wavelengths of light and produce more hydrogen compared to traditional methods.
Researchers at Kanazawa University used high-speed atomic force microscopy to study the TRPV1 protein's structural fluctuations in response to stimulating and suppressing ligands. They found that ligand binding increases conformational fluctuations, while suppression decreases them.
Researchers developed a novel method to predict antiviral drug targets by analyzing conformational changes in viral glycoproteins. The method, published in Journal of Computational Biology, identifies regions with high free energy, which may be promising for future antiviral drugs or vaccines.
Researchers have developed a new method to monitor molecular aggregation in real-time, allowing for the analysis of conformational changes. The method uses the AACD effect and chiral molecules to track aggregation-annihilation circular dichroism, providing valuable insights into biological processes.
Researchers investigated how bacteria like <i> Bacillus subtilis </i> respond to oxygen changes by studying protein HemAT. The study reveals a signal transduction chain that connects the sensor domain to the signalling domain, allowing the protein to transmit information about rising oxygen levels.
Researchers from TUM proved that Hsp90 utilizes thermal fluctuations as the driving force for its conformational changes. Key findings show that the chaperone protein is highly flexible and can switch between conformations using random environmental collisions, saving valuable ATP energy.
A lead-specific DNAzyme uses the 'lock and key' reaction mechanism, but switches to 'induced fit' in the presence of zinc or magnesium. This discovery could lead to faster and more sensitive sensors.
A research team led by Professor Timothy Zwier has demonstrated how laser light can be used to prompt large molecules to make alterations in their three-dimensional structure. By choosing different infrared wavelengths, the laser can selectively choose the molecule's new shape, favoring the formation of one conformation over another.