Articles tagged with Active Sites
Researchers developed a strategy to design single-atom catalysts for CO2 transformation, exhibiting superior activity and stability. The Ir-based catalyst shows the best performance yet for heterogeneous conversion of CO2 to formate.
Yale researchers used Google's algorithm to understand how information is transferred between enzyme sites, identifying crucial amino acids. This breakthrough could lead to new antibiotics, pesticides, and herbicides, combining data science with molecular dynamics simulations and NMR spectroscopy.
Researchers have developed a novel method to determine the cause of catalytic activity in complex catalysts, enabling better control over metal support interactions. The approach utilizes vertically grown carbon nanotubes as 'hydrogen highways' to separate active sites and optimize catalyst performance.
Researchers have identified a europium-containing enzyme in Methylacidiphilum fumariolicum SolV, which is essential for the bacterium's growth and catalyzes methanol conversion. The study reveals that the type of rare earth element bound affects enzyme activity.
A research team developed a more effective variant of an enzyme that can break down polyethylene terephthalate (PET), a common plastic used in bottles. The improved enzyme shows promise in degrading not only PET but also a bio-based substitute, polyethylene furandicarboxylate (PEF).
Researchers from NREL have pinpointed regions on enzymes that can be targeted via genetic engineering to break down cellulose faster. The team has gained a better understanding of the structure-activity relationships of these enzymes, which are crucial for industrial processes such as cellulosic ethanol production.
Researchers have created an alternative and cheapest anode material for excellent and ultra-stable alkaline water electrolysis. The new core-shell nanostructured electrocatalyst replaces precious metals, achieving highly efficient oxygen evolution activity and ultrastability.
Scientists at Washington University in St. Louis have developed the first experimental map of a cyanobacteria's water world, revealing pathways that could be used to deliver water to the active site. The discovery advances photosynthesis research and has implications for green fuels.
Researchers from the Hong Kong University of Science and Technology discovered a unique substrate-binding mode for OSB-CoA synthetase, a crucial enzyme in bacterial vitamin K biosynthesis. The study revealed distinct amino acid residues contributing to thioesterification half-reaction without affecting adenylation.
Researchers successfully resurrected Precambrian β-lactamases to study the emergence of primordial enzymes and explore the creation of novel active sites. The team demonstrated that ancestral protein resurrection enables the generation of new enzyme functions, overcoming current limitations in molecular biology.
The OU professor's research will integrate with educational and outreach programs for American Indian students, emphasizing the importance of sustainable energy. The study aims to quantify the role of catalytically active sites in biomass conversion processes.
A novel Fe-N/C catalyst with a silica-protective-layer approach has shown high oxygen reduction reaction activity comparable to platinum-based catalysts. The research paves the way for the commercialization of hydrogen fuel cells, potentially reducing costs and increasing efficiency.
Researchers describe chemical reactions responsible for hydrogen generation stability in aerobic environment by algal enzymes. They propose a new catalytic model that reveals two pathways for oxygen molecule penetration into the protein structure.
Researchers have gained insights into the molecular mechanisms behind bioluminescence in fireflies, click beetles and glow worms. Mutations to an enzyme called luciferase produce red light in acidic conditions, while changes favoring green light emission occur under normal conditions.
A new study reveals how LuxO, a key response regulator in Vibrio cholerae's quorum-sensing cascade, regulates the pathogenicity of the disease-causing bacterium. The researchers discovered an unusual inhibitory mechanism that permanently switches on LuxO, opening doors for potential therapeutic interventions.
Researchers have identified a structural weakness in antibiotic-resistant bacteria, revealing a potential therapeutic target. The analysis of four beta-lactamase enzymes found that their flexible structures are cooperatively correlated, making them vulnerable to disruption by small molecules.
Researchers found a small molecule that can convert an enzyme to more effectively metabolize acetaldehyde, reducing cancer risk. The study uses mice with defective ALDH2 enzymes and finds that a small molecule named Alda-89 increases the activity of ALDH3A1, a related enzyme.
Researchers at Princeton University have directly observed the electronic states of iron-sulfur clusters in enzymes, revealing an order of magnitude more accessible states than previously reported. This discovery presents many different chemical possibilities and could explain the ubiquity of these clusters in biological processes.
Researchers at EPFL have identified an alternative part of Abl-kinase on which drugs can bind with reduced risk of drug resistance. This new approach may overcome the problem of tumor drug resistance, offering a potential treatment for chronic myeloid leukemia.
Scientists developed a deeper understanding of ideal mesoporous nanoparticle design to maximize catalytic output. They modeled molecular movement within narrow channels and found that the optimal channel diameter balances pore size with reactant and product passage.
Researchers have discovered a crucial role of electronic and geometric effects in reducing carbon dioxide using gold-copper bimetallic nanoparticles. This breakthrough could lead to unprecedented improvements in electrochemical carbon dioxide reduction.
Researchers at DESY's PETRA III facility watched organic solar cells degrade in real time, revealing a mechanism of degradation that involves growth and receding of active domains. The study could lead to new approaches for increasing the stability of this promising type of solar cell.
Researchers at the University of Oulu, Finland, and the Helmholtz Center Berlin have shed light on the structure of thiolase, an enzyme crucial for lipid metabolism in parasites. By blocking the active site, lipid-like substances can be developed to inhibit parasitic metabolism.
A Penn team has developed a new class of malaria drugs by mimicking a natural reaction with a synthesized molecule, inhibiting the calpain enzyme. The innovation uses an alpha-helical shape to block the enzyme's activity, offering a highly specific and potentially safer alternative.
Elih Velázquez-Delgado uses X-ray crystallography to discover how nature inactivates caspase-6, a disease-related enzyme. He finds that deleting three specific amino acids reverses the effect and opens a door for developing a drug.
Researchers at Berkeley Lab have developed a technique to create molecular analogs of the active part of molybdenite, a widely used industrial catalyst. This method holds promise for creating catalytic materials that can generate hydrogen gas from acidic water at lower costs and with greater efficiency.
Scientists have developed a new approach to treating autoimmune diseases by creating artificial antibodies that target the MMP9 enzyme. These 'metallobodies' mimic natural inhibitors and selectively block two members of the MMP family, preventing symptoms in mice with inflammatory conditions.
Researchers solved the 40-year mystery of how desaturase enzymes insert double bonds in plant fatty acids. They discovered that a single amino acid, far from the enzyme's active site, can exert 'remote control' over double bond placement by binding to a carrier protein.
University of Virginia researchers have identified a new type of catalytic site for oxidation reactions, which could lead to the development of more efficient catalysts. The discovery was made using a combination of experimental and theoretical tools, including spectroscopy and computational chemistry.
Researchers at Scripps Research Institute found that an E. coli enzyme must move to function properly, and blocking these movements renders it defective. The study may lead to the development of more specific and effective drugs targeting enzymes.
Researchers at Harvard University found that similar molecular changes turned a harmless digestive enzyme into a toxin in two unrelated species, a shrew and a lizard. The study suggests that protein adaptation may be a highly predictable process, potentially leading to the discovery of other toxins across various species.
Researchers at Vanderbilt University Medical Center used NMR methods to determine the structure of diacylglycerol kinase (DAGK), a large bacterial protein that resides within the cell membrane. The study suggests that similar methods can be applied to other membrane proteins, including G protein-coupled receptors, which are targets for...
Scientists have developed a synthetic catalyst that mimics the active site of naturally occurring enzymes, which process hydrogen like platinum. The researchers created a model of the nickel-iron complex, including a bridging hydride ligand, to better understand the mechanism of hydrogenases.
Pol II selects correct NTPs to add to mRNA chains with exquisite precision, using a kinetic selection mechanism that involves the trigger loop. The study reveals how Pol II discriminates against incorrect NTPs and sheds light on the mechanisms of fidelity in cellular genetic copying machines.
Researchers at Fox Chase Cancer Center have identified a molecule, IPA-3, that can shut down PAK1, an enzyme involved in pathways leading to breast cancer. The molecule achieves high selectivity for PAK1 by binding to its auto-regulatory arm, preventing the enzyme from becoming active.
A team of scientists, led by UCSF's Brian Shoichet, successfully translated the structure of an enzyme into its function. By modifying a molecular docking technique, they predicted the natural molecule that triggers enzyme action, confirming the approach's potential to determine how key enzymes work in the body.
A Mayo Clinic researcher has identified a target site in malaria-carrying mosquitoes that could be used to develop toxic pesticides. The residues are found in three mosquito species and the German cockroach, but not in mammals.
A Mayo Clinic researcher has identified a unique enzyme residue in greenbugs and aphids that could be targeted by a new generation of pesticides. This discovery opens the door to creating safer pesticides that would not harm humans and animals.
A recent study by MIT chemist Catherine L. Drennan has discovered the simple secret behind how organisms create self-medications like antibiotics and anti-tumor agents. The enzyme SyrB2, which uses a smaller amino acid to bind halides, reveals an elegant simplicity in its mechanism.
A new computer program called CPDL identifies candidate amino acid sites that control protein functions by comparing groups of related proteins. The tool flags positions where two related groups differ in terms of amino acid identity or properties like charge or polarity, suggesting these sites are biologically important for defining s...
Researchers at UCSD have identified a promising set of inhibitors that may overcome drawbacks of previous compounds. The new molecules are less likely to cause side effects, such as one being the food additive Maltol.
Researchers at Brookhaven National Laboratory have deciphered the structure of botulinum toxin, shedding light on its mechanism of action. By modifying a single amino acid, scientists created an inactive form of the toxin that retains structural similarity to the active form, paving the way for potential vaccine development.
Researchers used molecular modeling to study the detoxifying proteins of black swallowtail butterflies and corn earworms. The earworm's protein is more flexible, allowing it to bind to and detoxify six different plant defense chemicals and three common insecticides, making it a master of adapting to new pesticides and host plants.
Virus researchers discovered a critical role of Z-DNA in pox virus lethality, leading to potential development of anti-viral compounds effective against smallpox. The findings may also shed light on the regulation of transcription and cellular responses to viral infections.
Resistant strains of Staphylococcus aureus, also known as hospital staph, have become increasingly prevalent worldwide. Researchers have identified key differences in the structure of penicillin-binding protein 2A (PBP2a), which enables it to resist beta-lactam antibiotics.
Researchers at Brookhaven Lab have identified a new approach to developing antiviral agents by targeting the protease enzyme used by adenoviruses. The three-pronged therapy approach may overcome drug resistance, as mutations affecting one site are less likely to affect others.
Researchers have identified mutant enzymes with improved detoxifying properties against chemical warfare agents and agricultural insecticides. By modifying amino acids, the team has created faster-detoxifying enzymes that can efficiently degrade these compounds.
Scientists propose a revised four-point location model to explain how proteins discriminate between mirror-image molecules. This new understanding could significantly impact drug design, as it challenges the long-held three-point attachment model and may lead to more effective treatment strategies.
Researchers solved the crystal structure of human tumor necrosis factor-alpha-converting enzyme (TACE), revealing its unique features and providing insights into its role in inflammatory diseases. The study's findings have significant implications for developing targeted therapies for rheumatoid arthritis and septic shock.