A novel light-manipulating technology using nanodisk periodic structures has been developed by an international team, including Kyoto University. By controlling bound states in the continuum, researchers can systematically control light distribution states and manipulate near-infrared light within a nanodisk.
Researchers found that many proteins thought to be monomeric exist as hexamers or other shapes, with some even forming tetramers. This discovery suggests a high degree of structural plasticity among proteins.
Australian researchers have discovered a new mechanism by which T cells can react to lower doses of antigens, leading to a 50-fold increase in T cell activation sensitivity. This finding opens up new possibilities for developing more effective immunotherapies.
Scientists at the University of Tsukuba developed a method to produce uniform, hollow vessel-shaped crystals through spontaneous crystal growth. The crystals have hexagonal symmetry and can be used as tiny containers for nanotechnology experiments.
Researchers used x-ray crystallography to study the main protease of SARS-CoV-2 at various temperatures, revealing subtle conformational changes and potential targets for drug design. These findings may inspire the development of new antiviral drugs to counteract COVID-19 and prevent future pandemics.
Researchers developed a monoclonal antibody that binds E-cadherin, strengthening cell adhesion and preventing cancer metastasis. The antibody, 19A11, has two binding modes that increase adhesive strength through salt bridge formation.
The study reveals how the protein binds to ligands and inhibitory antibodies, providing insights into its molecular function. The findings may lead to better targeted therapeutic approaches in the future.
Herbicide companies are shifting their research focus to address growing resistance, using AI, X-ray crystallography, and computer simulations to predict target enzymes and inhibit herbicides. This could lead to new commercial products, but experts caution farmers to moderate use and consider additional crop protection tools.
Researchers used X-ray crystallography to reveal the structure of HIV-1 matrix protein at 2.1 angstroms resolution, advancing understanding of viral assembly and envelope protein incorporation. The study showed that molecular details at this level can help develop new therapeutic agents inhibiting HIV-1 assembly and virus production.
Researchers elucidated the protease-inhibitory mechanism of A2ML1 using cryo-EM structures, shedding light on its role in severe autoimmune blistering diseases. The study improves understanding of related proteins and their function.
Scientists employed artificial intelligence to determine the 3D structure of the VP8* B domain in group B rotavirus, a crucial step towards understanding its interaction with host cells and developing new treatments. The newly described structure reveals unique sugar recognition capabilities, distinct from other rotaviruses.
A research team from the University of Bayreuth has successfully generated and analyzed materials under compression pressures of over 1 terapascal, a breakthrough that could deepen our understanding of matter. The study reveals the synthesis and structural analysis of novel rhenium compounds in the terapascal range.
A study by Rice University bioscientists has revealed the presence of a central metal ion critical to DNA replication and implicated in misincorporation. The research found that three metal ions are involved in the process, with the first supporting nucleotide binding and the second stabilizing the binding of loose nucleotides. This di...
Researchers have developed a new approach to studying RNA molecules using nanotechnology and cryo-electron microscopy (cryo-EM), enabling the analysis of RNA subunits with unprecedented resolution. This breakthrough has significant implications for fundamental research, drug development, and RNA therapeutics.
A new study reveals that two equal charges in enzymes do not repel each other, but instead attract, facilitating chemical reactions. The researchers used protein crystallography to obtain a structural snapshot of the substrate before the reaction and found an attractive interaction between the enzyme and substrate.
Researchers have solved the structure of class II PI3Kα, a promising target for anticancer drugs, and discovered its activation mechanism. Inhibition of this enzyme could help patients with tumor growth and angiogenesis.
The study reveals a novel technique using ammonium ions to observe ions in the selectivity filter of ion channels for the first time. This breakthrough enables researchers to investigate pharmacological effects and gain new perspectives on ion channel research.
Researchers have discovered the structure of C.difficile's protective armor, a chain-mail like layer that prevents molecules from entering the cell. This discovery opens the possibility of designing specific drugs to target the armor and kill the cell.
Scientists at Stanford University and SLAC National Accelerator Laboratory have created a molecular cage to study the structure of KIX, a protein used by AML cancer cells. The technique has successfully imaged KIX with cryo-EM, revealing new insights into its function and potential targets for therapy.
Researchers have discovered an ancient receptor protein that can detect karrikins in smoke from burnt plant material, initiating molecular signals to speed up seed germination. The study also found that the receptors play a role in sensing growth hormones in plants, shedding light on the enigmatic karrikin signaling pathway.
A new material, sodium carbo-hydridoborate, improves the performance of solid-state sodium batteries, making them more sustainable and durable. The ideal pressure to be applied to the battery for efficient operation has also been defined.
A study led by Przemyslaw Nogly at PSI has detailed insight into the mechanism of a light-driven chloride pump in bacteria, revealing how light energy converts to kinetic energy and transports chloride ions inside cells. The pump uses two molecular gates to ensure one-way transport, with the process taking around 100 milliseconds.
A team of scientists at Brookhaven National Laboratory has identified a molecule with significant potential to disable the COVID-19 virus. The molecule was discovered using high-throughput virtual screening and laboratory experiments, and its ability to bind to the virus's main protease was confirmed through structural studies.
Researchers develop small-molecule serial femtosecond crystallography, enabling precise analysis of complex materials. The technique reveals accurate atomic structures of previously unsolvable compounds.
Researchers identified a mechanism by which two antiviral genes, SAMD9 and SAMD9L, promote childhood cancer when mutated. The study found that this protein region performs the toxic function through binding to nucleic acids.
Scientists have developed a new technique called small-molecule serial femtosecond X-ray crystallography (smSFX) that can reveal the structures of not-so-neat-and-tidy materials. This method uses an exceptional X-ray laser and custom-built image processing algorithms to diffract individual granules of powders, providing a precise sharp...
Researchers have developed a new approach to determine the structures of tiny crystals relevant to chemistry and materials science. The new method, called smSFX, uses ultrafast pulses from an X-ray free-electron laser to collect structural information before damage sets in.
Researchers developed propSym to calculate fundamental constants of solids, reducing redundant components and improving material modeling. The open-source software is adaptable to various physical properties, aiming to lower the entry barrier for analytical modeling.
Scientists at Osaka Prefecture University have identified specific parts of the dog allergen Can f 1 that can trigger an immune response in people. The researchers used X-ray crystallography to determine the structure of the protein and found several potential epitopes, or regions, that could be targeted by a vaccine.
A team of researchers at UC Santa Cruz has created an unusual protein structure known as a ‘rippled beta sheet’ by mixing mirror-image peptides. The study used x-ray crystallography to obtain images of the structure, which closely matches predictions made in 1953 by Linus Pauling and Robert Corey.
Researchers used room-temperature crystallography to study photosynthetic bacteria's proteins, discovering they are 'remarkably robust' and more efficient than previously thought. The study sheds new insight into the mechanism of electron transfer early in photosynthesis.
Scientists have discovered a new potential treatment to reverse antibiotic resistance in bacteria causing sepsis, pneumonia, and urinary tract infections. The indole carboxylates class of enzyme blockers can stop MBL resistance enzymes from working, allowing antibiotics like carbapenems to effectively target bacteria.
Scientists at Queen's University Belfast have developed a computer-aided data tool that can predict novel sites of binding for potential drugs. The tool aims to improve treatment for a range of illnesses by increasing therapeutic efficacy and reducing side effects.
Researchers from South Ural State University discovered the reasons for the stability of salts, attributing it to the properties of electron density distribution. The study reveals the importance of chemical bonding in multi-centre character, paving the way for predicting material properties.
McGill researchers have discovered how bacteria create cyanophycin granules, a reserve of nitrogen and energy. The study uses cryo-electron microscopy and X-ray crystallography to visualize the active enzyme in action, opening up possibilities for biotech applications.
Researchers at Aarhus University have elucidated structures of a sugar transport protein that drives transport of sugar in plants, revealing key elements involved in the transport cycle. The study provides new evidence for regulatory mechanisms conserved within the sugar porter family across all kingdoms of life.
Scientists have elucidated and visualized the 3D molecular structure of the melanocortin 4 receptor (MC4R), a crucial component of appetite regulation. The study's findings provide insights into the protein's interaction with hormones and potential targets for drug interventions to treat severe obesity.
Researchers have developed a new method for preparing cryo-electron microscopy samples using liquid nitrogen, which cools at rates roughly 50 times slower than ethane. This results in sharper images with reduced beam-induced motion and simplified workflows.
Scientists have identified tube-forming proteins in mycobacterial outer envelope that enable protein secretion. The discovery, using x-ray crystallography and cryo-electron microscopy, reveals a novel method for studying substance transport mechanisms in pathogenic mycobacteria.
Researchers at Berkeley Lab have made significant breakthroughs in developing a highly effective COVID-19 antibody therapy and an efficient thermoelectric system that can convert waste heat to electricity. The new antibody, S309, has been shown to neutralize all known SARS-CoV-2 strains and may be more difficult for new mutants to escape.
The new animations create a visual representation of cell respiration, showcasing the breakdown of glucose and release of energy. The animations were built using cutting-edge scientific discovery and research, including models from X-ray crystallography and molecular dynamics simulation.
A team of researchers from Tokyo Institute of Technology developed a novel imaging method using metal-atom tracers in HAADF-STEM to determine the conformational structures of complex polynuclear coordination compounds. The technique achieves accurate visualization of highly branched molecules, filling a gap in structural analysis.
Researchers have developed a neural network model called BiteNetPp to detect protein-peptide binding sites, enabling the design of peptide-based drugs. The model consistently outperforms existing methods and can analyze a single protein structure in under a second, making it suitable for large-scale studies.
The study describes the three-dimensional structure of the MUTYH protein and its interaction with PCNA, a key player in DNA replication. The researchers found that mutations in the MUTYH gene reduce its binding affinity to DNA and destabilize its structure, leading to decreased DNA repair activity.
Scientists successfully produce and characterize a crystalline complex with a two-dimensional equivalent of silicon, defying geometric expectations. The resulting structure displays surprising physical and chemical properties, opening up new avenues for catalysis and materials research.
UT Southwestern researchers report the first structural confirmation that endogenous molecules can trigger innate immunity in mammals through the TLR4?MD-2 receptor complex. The discovery has wide-ranging implications for treating and preventing autoimmune diseases such as multiple sclerosis.
The AlphaFold Protein Structure Database provides the most accurate and complete picture of human proteins, enabling researchers to accelerate discovery and advance scientific knowledge. The database covers all ~20,000 human proteins and offers a treasure trove of data that could unlock future advances in AI-enabled biology.
Researchers introduce RoseTTAFold, a neural network approach that accurately predicts protein structures, outperforming traditional methods and rivalling DeepMind's AlphaFold2. The tool's code and public server are now accessible to the scientific community, enabling rapid solution of challenging structure determination problems.
Researchers from Institut Pasteur and CNRS discover the biosynthesis pathway of 2-aminoadenine, a new base in DNA, using crystallography platform. The discovery increases coding bases in DNA, enabling synthetic genetic biopolymers.
Researchers at Skoltech have successfully synthesized two new ternary hydrides, LaH10 and YH10, which are expected to exhibit high-temperature superconductivity. The study reveals that alloying is an effective strategy for stabilizing these otherwise unstable phases.
Scientists have discovered a new mineral, allabogdanite, at the Dead Sea that was previously only found in meteorites. The discovery has implications for our understanding of Earth's surface conditions and geological processes.
Researchers created designed and biologically active 2-D and 3-D protein arrays using DNA-based assembly, maintaining structural stability and biological activity. The method has potential applications in structural biology, biomaterials, nanomedicine, and biocatalysis.
A German-Japanese research team has deciphered the 3D structure of a metalloprotein that catalyzes RNA editing in all plant cells. The DYW domain's activation is triggered by a zinc atom and a gating domain, providing a sophisticated regulation mechanism for chloroplasts and mitochondria.
Scientists at Weill Cornell Medicine developed a computational technique that greatly increases the resolution of atomic force microscopy, revealing atomic-level details on proteins and biological structures. The new method allows researchers to study biological molecules under physiologically relevant conditions, providing high-resolu...
A new study combines experimental data and molecular dynamics simulations to study the conformation of an RNA fragment involved in protein synthesis. The research led to a new method for defining biomolecule structures in their physiological environments.
Researchers elucidated the molecular structure of RcaE, a representative cyanobacterial photosensor, revealing its unique conformation and potential proton transfer route to bilin. The study provides insights into how cyanobacteria evolved diverse spectral sensitivities and contributes to the development of new photoswitches.
A team of scientists found that the human 14-3-3 protein family has a universal binding site for the E6 oncoprotein from different subtypes of cancer-causing Human Papillomaviruses (HPV). This discovery suggests that targeting this site could lead to the development of novel antiviral therapies.
Researchers have identified a hidden region on the SARS-CoV-2 Spike protein that is masked by metabolites, making it inaccessible to antibodies. This finding highlights the importance of targeting this region in developing new vaccines.
Researchers have identified a new light-driven enzyme, fatty acid photodecarboxylase (FAP), that converts fatty acids into alkanes and alkenes under blue light. The enzyme's complex photocycle drives this transformation, and its structure has been elucidated using serial femtosecond crystallography.
Researchers found biliverdin and bilirubin, natural molecules present in the body, can suppress antibody binding to SARS-CoV-2. This discovery may help explain why some COVID-19 patients become severely ill despite having high levels of antibodies against the virus.