Researchers used quantum mechanics and supercomputing to study the surface structure of rutile TiO2, a promising photocatalyst. The study identified new structures and processes that can enhance its chemical reactivity.
Scientists have made a breakthrough in visualizing proteins involved in cancer cell metabolism using cryo-EM. They were able to capture images of glutamate dehydrogenase at an atomic level, revealing new insights into potential drug targets. This discovery has the potential to revolutionize and accelerate the drug discovery process.
Researchers at UT Southwestern Medical Center have determined the 3D atomic structure of a human sterol transporter that helps maintain cholesterol balance. This knowledge could lead to finding highly targeted therapies to treat or prevent diseases related to sterol imbalance.
Researchers at Princeton University have revealed new insights into the mechanism of phenylalanine hydroxylase, a critical liver enzyme for human health. By applying unique approaches combining small-angle x-ray scattering and chromatography, they provided evidence for a model of the active structure of the enzyme.
A new study by UNIST researchers has observed structural changes in carbonic anhydrase for the first time. The enzyme catalyzes a reaction converting CO2 and water into protons and bicarbonate ions at a rate of 106 reactions per second, crucial for regulating chemical environments.
A team of researchers used neutron crystallography to better understand a protein implicated in HIV replication, revealing a pH-induced proton 'hopping' mechanism that guides the enzyme's activity. This understanding is vital for drug resistance and guiding rational drug design.
The study reveals that the calcium pump uses energy from ATP to transport calcium ions into the cell, a process crucial for muscle function and heart health. This insight could lead to the development of new drugs targeting this enzyme to alleviate ionic imbalances associated with disease.
A team of researchers has developed a method to image molecular movement in real-time, revealing the fundamental processes of a chemical reaction. This breakthrough allows scientists to study the structure and behavior of proteins at the atomic level, shedding light on the chemistry necessary for life.
Researchers at Umea University and Swedish Defence Research Agency develop a three-dimensional structure of the HI-6 nerve agent antidote, revealing its binding mechanism to acetylcholinesterase. The breakthrough provides new insights into designing effective antidotes against sarin and other nerve agents.
Researchers obtained images of the NMDA receptor in active, non-active, and inhibited states using x-ray crystallography and single-particle electron cryomicroscopy. The study reveals the complex movements of the receptor's subdomains during activation and provides insights into designing novel therapeutic compounds.
Researchers created an efficient diode-pumped eye-safe laser using GdAl3 single crystals co-doped with Er and Yb. The laser emits safe wavelengths for human eyes and has advantages in telecoms due to low atmospheric losses.
Researchers at the University of Michigan are developing a new strategy to combat cancer metastasis by targeting an enzyme called P-Rex1. Tumor cells produce high levels of P-Rex1, allowing them to spread and become mobile.
Researchers discovered slow-binding inhibitors (SBIs) with high selectivity, long target-residence times, and minimal side effects for treating Alzheimer's disease, myasthenia, and neuroprotection. SBIs also have toxicological importance, playing a role in mechanisms of resistance against irreversible agents.
Researchers have developed hybrid pixel array detectors that can achieve low noise for single-photon detection and spectroscopic imaging. The new technology uses standard components, enabling the creation of larger and more optimized systems.
Scientists create a 'hollow' version of the plant virus cowpea mosaic virus (CPMV) which can be used as a carrier for drug molecules. This finding opens up new possibilities for cancer treatment and vaccine design.
A new 3-D modeling and data-extraction technique can reveal dynamics in protein crystals, improving the clarity of imaging and providing valuable information about protein motions. This approach has potential benefits for pharmaceutical industry and structural biology.
A French research team, led by Dr. Frédéric Leroy, has created a method for real-time monitoring of surface changes at the atomic level. The approach enables them to study the kinetics of silicon dioxide decomposition onto silicon during thermal treatment, revealing a non-homogeneous process involving hole nucleation and opening.
Enrico Di Cera's work on the Structural Biology Data Grid allows researchers to share and reproduce findings faster, advancing the field of structural biology. The grid supports archiving of raw experimental datasets, enabling rapid access for validation and improving existing models.
Researchers have developed a new method to determine the structures of nanocrystalline pharmaceuticals, reducing radiation damage and allowing for study at room temperature. The approach uses low-dose electron diffraction with a high-sensitivity detector, enabling the collection of high-quality data for direct crystallography methods.
Researchers have identified the three-dimensional structure of a hantavirus protein, providing a promising model for developing drugs against the disease. The protein's circular complexes may play a role in inhibiting viral growth, making it an ideal target for future treatments.
Orion Berryman, a UM assistant professor, has received a $675,000 CAREER grant to study multidentate halogen bond donors for supramolecular catalysis. He will use the award to design molecules that complement sulfur compounds and teach students about chemical concepts through 3-D printing.
This review article presents an extended study on the crystal and magnetic structure of multiferroic hexagonal manganite RMnO3, which exhibits ferroelectric and magnetic orders. The research highlights the importance of strong interactions between these orders, leading to unique properties.
Researchers develop a new technique to determine the spatial structures of proteins and molecules without prior knowledge, revolutionizing crystallography. The method provides insights into the modes of action of biomolecules and can lead to tailor-made drugs for diseases.
Researchers have developed a new method to obtain high-resolution molecular images using continuous diffraction patterns in imperfect crystals. This approach allows for better structural detail and could revolutionize the study of complex biological machinery, including photosynthesis and catalysis.
A team of scientists has produced a structural movie showing the creation of S-Adenosylmethionine (SAMe), a major methyl donor in the body that plays a role in some cancers. The research provides insight into how this enzyme synthesizes SAMe and highlights it as an excellent therapeutic target for cancer treatment.
Researchers propose using twisted X-rays to study non-crystalline but symmetric structures like helices. This method matches the symmetry of incoming radiation to the structure's symmetry, producing sharp peaks in diffraction data that can be used for accurate structure prediction.
Researchers at Karolinska Institutet have determined the 3D structure of Juno, a mammalian egg protein essential for triggering gamete fusion. The study reveals that changes in Juno's shape alter its ability to bind with sperm protein Izumo1, bringing scientists closer to understanding fertilization.
Scientists at Stockholm University have successfully determined the structure of the sodium/proton transporter NapA using x-ray crystallography. This breakthrough provides a complete picture of the transport process, revealing key movements and steps involved in regulating sodium levels within cells.
Researchers found that fluoroquinolones interact with an enzyme in TB germs, but not as strongly as thought. They discovered a new way to make the drugs more potent by targeting broken DNA within the gyrase complex. This could lead to improved treatments for multidrug-resistant TB and other bacterial infections.
The Biophysical Society has announced the winners of its annual CPOW Travel Awards to increase women biophysicists' participation at the 2016 Annual Meeting. The recipients include Jana Broecker, Nabanita Das, and others presenting posters or oral presentations on various membrane proteins and calcium signaling.
Researchers have successfully mapped the structural map of a tiny cellular nanomachine called diacylglycerol kinase, which plays a critical role in bacterial cell wall synthesis. The nanomachine's evolution is an extraordinary feat of nature, and its molecular blueprint has shed new light on how it performs its cellular duties.
Research at INRS demonstrates that small changes in enzyme structure can significantly impact its function. The study reveals how the subtle dance of atoms affects enzyme activity, shedding light on protein engineering failures and improving synthetic functional enzymes.
Researchers at TSRI have discovered the dynamics of β2 adrenergic receptor (β2AR), a protein linked to asthma, obesity and type 2 diabetes. The study found that β2AR naturally fluctuates between its active and inactive states in the absence of any drug, and different drugs can either stimulate or inhibit signaling.
Research reveals how Bdellovibrio bacteriovorus uses an ankyrin-type protein called Bd3460 as a shield to protect itself against its own enzymes. The study found that the protein binds to the tip of the enzyme weapons, nullifying their action until they are safely secreted out of the Bdellovibrio and into the prey bacteria.
Scientists discovered a 'master switch' in cancer cells that allows them to survive stress conditions by overriding the normal stress response. The Brf2 protein acts as a sensor and regulates gene activity, enabling cancer cells to thrive under stress.
Researchers discovered a 'self-protection' protein in predatory bacteria that binds to enzymes, temporarily deactivating them. This mechanism helps Bdellovibrio bacteriovorus protect itself from its own attack while killing other bacteria.
Researchers have created a detailed image of pneumolysin, a toxin linked to deadly infections like pneumonia and meningitis. The structure reveals how the toxin assembles on cell surfaces, enabling the development of novel therapeutic approaches to block its formation.
Researchers developed a new method to study metal-organic frameworks (MOFs) storing gases, revealing cooperative gas-gas interactions and superlattice structures. The discovery holds promise for designing more efficient MOFs for carbon capture and hydrogen fuels.
Complex engineered materials pose significant structural challenges due to non-periodic and disordered atomic structures. A new approach combining experimental and theoretical tools is required to obtain unique solutions.
Researchers at Griffith University's Institute for Glycomics have determined the first three-dimensional image of a protein involved in cancer spread using X-ray crystallography. The study reveals the enzyme heparanase, which degrades a sugar molecule and is associated with angiogenesis, inflammation, and increased metastatic potential.
A recent study published in PNAS has shed light on the mechanism of action of HigB, a bacterial toxin that contributes to antibiotic resistance. The researchers found that HigB selectively degrades specific mRNAs, leading to the formation of persister cells that are tolerant to antibiotics.
A type of bacteria, Thiomicrospira crunogena, produces an enzyme, carbonic anhydrase, that can convert industrial carbon dioxide into bicarbonate. The enzyme has high thermal stability and could be used in industrial settings to neutralize greenhouse gases.
Researchers at the University of Florida have identified a type of deep-sea bacteria that can convert industrial carbon dioxide into bicarbonate, a process that could help neutralize greenhouse gases. The enzyme produced by the bacterium has high thermal stability, making it suitable for industrial applications.
The COMPASS method uses a combination of molecular spectroscopy techniques, predictive protein-folding algorithms, and image recognition software to determine a protein's likely structure. The approach has been successfully applied to 15 proteins and holds promise for studying complex protein structures that have eluded researchers.
Researchers at Hiroshima University discovered that Sendai virus C protein inhibits STAT1 activation after interferon stimulation, enabling the virus to evade the host immune response. This finding opens up new avenues for developing anti-viral drugs to overcome damage caused by interferons.
Researchers used X-ray crystallography, NMR and simulation to study protein movements in crystals. The results show that proteins continue to produce slight residual movements even when crystallised, which blurs the structures obtained via crystallography.
Researchers identify and map a light-sensing protein that uses vitamin B12 to regulate gene expression in response to light exposure. The discovery expands the biological role of vitamin B12 and offers insights into novel modes of gene regulation.
Researchers have obtained the first nanometer-resolved image of individual tobacco mosaic virions using low-energy electron holography, a non-destructive single-particle imaging technique. This breakthrough could lead to improved drug design by providing detailed knowledge of biomolecular structures.
Researchers at Rice University and Baylor College of Medicine have successfully mapped the structural details of leiomodin 2, a protein critical to muscle cell function. The discovery offers a path forward for studying and treating nemaline myopathy, a hereditary disorder that weakens muscles.
Researchers developed a rotaxane gold catalyst with enhanced properties, which can be controlled by adding acid or metal ion cofactors. The catalyst's shape changes with different ions, leading to varied reaction products and suggesting a potential method for tailoring catalysts.
A new tool, phenix.diffuse, enables calculating diffuse scattering from Protein Data Bank-formatted structural ensembles, addressing the need for computational modelling and validation tools. The technique helps extract evidence of concerted motion in single crystal forms, where high-quality data sets are limited by long X-ray exposures.
Scientists at UCLA used a microscope to image the 3D positions of individual atoms with precision of 19 trillionths of a meter. This breakthrough enables researchers to infer macroscopic material properties from atomic arrangements, guiding the development of aircraft components and other applications.
A new method called Phantom Derivative (PhD) has been developed to determine complex structures with limited experimental data. PhD is a competitive approach in protein crystallography, producing results comparable to existing techniques like density-modification and Vive la Difference.
SLU researcher Nicola Pozzi is seeking to understand the molecular mechanisms of prothrombin and thrombin to develop more effective life-saving drugs. The research builds on previous breakthroughs in blood-clotting protein structure, which may lead to a better understanding of how prothrombin is converted to thrombin.
Researchers elucidated dynamin's role in forming a screw-like structure to constrict and release vesicles. Specific mutations impairing dynamin function are linked to congenital muscle disorders.
Researchers uncover structural details of how proteins interact to turn two signals into one, enabling fine-tuning of signal and drug action. The study provides crucial insights into nuclear receptor communication, paving the way for improved drug design.
A team of scientists has discovered how a plant sensor detects pathogens, bringing unprecedented detail to the 'gene-for-gene' hypothesis. The study reveals that the strength of binding between the sensor and pathogen proteins correlates with the plant's response, opening up new strategies for engineering enhanced resistance.
Scientists have finally understood the structure of a flexible plant virus that has resisted description for over 75 years, revolutionizing efforts to stop such viruses and potentially leading to new vaccine delivery methods.
Researchers in China have developed tiny nanocrystals that can specifically target and identify cancer cells, potentially leading to earlier diagnosis and treatment. The nanocrystals, made from heavy metals lanthanum and europium, can be used as 'staining' agents to highlight diseased cells under a microscope.
Researchers have discovered how bacteria convert phosphonate compounds into phosphate, using a complex of fourteen proteins. This mechanism could be used to develop techniques for removing pesticide residues from drinking water and understanding the greenhouse effect.