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.
SourceThe University of Osaka·JournalNature Communications·TypeExperimental study·DateJul 1, 2026
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.
SourceXi'an Jiaotong-Liverpool University·JournalApplied Surface Science·TypeExperimental study·DateJun 11, 2023
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.
SourceKanazawa University·JournalProceedings of the National Academy of Sciences·DateMay 14, 2023
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.
SourceMary Ann Liebert, Inc./Genetic Engineering News·JournalJournal of Computational Biology·DateApr 20, 2020
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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.
SourceHong Kong University of Science and Technology·JournalNature Communications·DateJan 11, 2019
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.
SourceRuhr-University Bochum·JournalJournal of Biological Chemistry·DateJun 25, 2012
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.
SourceTechnical University of Munich (TUM)·JournalProceedings of the National Academy of Sciences·DateJan 13, 2012
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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.
SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalNature Chemical Biology·DateNov 12, 2007
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.