Researchers at UT Southwestern Medical Center have mapped the atomic-level architecture of the CLOCK complex, a key component of the body's circadian rhythm. The study provides insights into how this protein works and may lead to better treatments for insomnia, diabetes, and cancer.
An international team led by SLAC National Accelerator Laboratory has used the world's most powerful X-ray laser to obtain ultrahigh-resolution views of nano-crystals of biomolecules, including a small protein found in egg whites. This technique enables researchers to view molecular dynamics at a time-scale never observed before.
Scientists have successfully imaged biomolecules at individual atom level using X-ray lasers, enabling new avenues for biological research. The technique, known as serial femtosecond crystallography, has been used to study a small protein called lysozyme and holds promise for understanding complex biological systems.
Scientists used a novel X-ray technique to analyze the structure of hen egg white lysozyme at a high resolution of 0.19 nanometres, demonstrating the potential of free-electron lasers in structural biology. The technique, which uses ultrashort X-ray pulses, enables the study of previously intractable molecular structures.
Scientists have developed a method to analyze noisy X-ray data, revealing details of molecular structure previously discarded due to low signal quality. This breakthrough could lead to more accurate models and improved understanding in biology, medical diagnostics, nanotechnology and other fields.
Researchers have elucidated the structure of type III secretion system needles at atomic resolution, revealing similarities in their inner part while surface variability evades host recognition. This discovery enables new insights into pathogen immune evasion and prospects tailored antiinfectives to block needle assembly.
Researchers at the University of Sheffield have defined the structure of the human obesity receptor, a key factor in regulating body fat. This breakthrough could lead to new treatments for complications of obesity and anorexia.
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 have identified metastasin as a crucial protein that helps stop tumor cells from spreading. By understanding how metastasin binds to motor proteins, scientists can develop drugs to block this interaction and prevent tumor cell proliferation.
Researchers at UCLA have developed a new method for directly measuring the atomic structure of nanomaterials, enabling 3D imaging of individual atoms. The technique, known as electron tomography, allows scientists to visualize the interior structure of nanoparticles in unprecedented detail.
A new solid state NMR method helps visualize protein shapes, aiding understanding of biological molecules' functions and behaviors.
Researchers at Baylor College of Medicine have developed a semi-automated protocol called pathwalking to generate initial models of protein folds from near-atomic resolution images. This approach enables the rapid generation of ensemble models that can be optimized for full atomic models.
Two research teams report new findings on the structure of enterovirus 71, a virus causing hand, foot and mouth disease and potentially fatal brain swelling. Researchers propose designs for antiviral drugs to treat the infection by targeting a unique 'pocket factor' exposed in EV71.
Mayo Clinic researchers have gained insights into the function of a histone chaperone called Rtt106 using NMR spectroscopy and X-ray crystallography. The study reveals two novel domains in Rtt106 that enable it to interact with modified histones, promoting proper chromatin assembly and disassembly.
Researchers determined the crystal structure of a critical control element within chaperonin, which promotes correct protein folding. The discovery sheds light on how proteins fold correctly and may lead to engineering modified protein-folding activities to combat diseases.
Researchers at Arizona State University have created an imaging technique that allows for atomic-level resolution without damaging biological samples. This breakthrough enables the use of high-intensity X-rays, previously limited by damage caused by the radiation.
Researchers at EMBL Hamburg used advanced techniques to study myomesin's three-dimensional structure and its role in maintaining muscle fibers. The discovery sheds light on the protein's function in living organisms, particularly in animal models.
Researchers are exploring X-ray imaging as a next-generation tool for gathering detailed structural and functional information on biomolecules. The technology has the potential to surpass traditional X-ray crystallography, enabling the study of complex biological systems in unprecedented detail.
Scientists at EMBL Hamburg have discovered the myomesin protein can stretch up to two-and-a-half times its length, unfolding in a previously unknown way. The study reveals the protein's superhelical architecture and unusual elastic properties, shedding new light on muscle contraction mechanisms.
Researchers have discovered a new porous zeolite material that can convert gasoline directly into diesel, offering a potential solution to the growing demand for diesel. The ITQ-39 material has complex atomic structure and channels of varying size and shape, enabling efficient conversion.
Researchers at Brandeis University have made a significant discovery on how EmrE, a protein responsible for exporting antibiotics from cells, works. By studying its structure and function using nuclear magnetic resonance spectroscopy, the team hopes to develop inhibitors that can target this protein and prevent drug resistance.
Researchers identified a three-dimensional crystal structure of the Abies grandis α-bisabolene synthase, an enzyme that produces bisabolene, a precursor to bisabolane. This breakthrough could lead to improved catalytic efficiency and stability, enabling microbes to produce bisabolene faster.
Researchers have discovered that proteins and ligands engage in a complex dance-like interaction, influencing the binding modes of ligands and receptor dynamics. This finding has implications for designing future diabetes treatments.
A UC Davis School of Medicine researcher has developed an algorithm that predicts the conformation changes in voltage-gated sodium channels, crucial for designing new drugs to treat chronic pain and epilepsy. This innovation could lead to highly specific and effective therapies with minimal side effects.
Carnegie Mellon researchers successfully used NMR to determine the structure of infinitesimal gold nanoparticles, revealing their handedness. This approach offers a significant advantage over routine methods for analyzing gold nanoparticles and holds promise for developing safer, more effective drugs.
A recent Van Andel Research Institute study found that decanoic acid acts as a modulator of PPAR receptors, which play a key role in glucose and lipid metabolism. The findings suggest that decanoic acid could be used to design better and safer PPARγ-based drugs for diabetes treatment.
Researchers developed a new technique to improve X-ray crystallography, allowing for three to five times better signal levels than standard methods. This enables the study of large molecules with greater depth and understanding while minimizing radiation damage.
Researchers have for the first time obtained an image of the structure and arrangement of apoA-I molecules using x-ray crystallography. This breakthrough may lead to the development of new drugs to treat diseases such as atherosclerosis and cardiovascular disease.
Researchers have deciphered the structure of an essential enzyme in photosynthetic organisms, a target for algaecide development. This discovery could lead to the creation of compounds that block the enzyme's function, inhibiting algae growth without harming other plant life.
The U.S. Department of Energy's national laboratories enabled the discovery of a groundbreaking new drug treatment for malignant melanoma, with FDA-approved drug Zelboraf (vemurafenib) showing great promise in disrupting disease progression.
Researchers at The Donald Danforth Plant Science Center have discovered that green tea polyphenols can control a deadly congenital disease by hijacking the ADP activation site. This finding has also been validated in two types of tumors, glioblastomas and tuberous sclerosis complex disorder, suggesting potential for drug development.
Researchers have defined the atomic structure of astrovirus, which causes juvenile diarrhea, identifying potential targets for vaccine development and antiviral drugs. The study may help block the virus before it becomes infectious and reduce the risk of dehydration in children.
Researchers discovered that gold bridges composed of a single atom are stiffest, contrary to everyday intuition. This finding is crucial for understanding the behavior of tiny components in devices like computer circuits.
A newly synthesized protein is fragile and requires chaperones for proper folding, which also escort it to its destination and aid in membrane insertion. The researchers identified key components responsible for TA protein sorting, including Get3 ATPase and receptors Get1 and Get2.
Scientists have gained a deeper understanding of how cells translate genetic information into proteins and processes by deciphering the Mediator protein structure. The research provides an important link to discoveries in the field and has the potential to lead to new treatments for disease.
Researchers at University of Michigan developed a new way to search for drugs that target RNA, a molecule essential to retroviruses like HIV. They successfully predicted the binding of six new small molecules to HIV's genetic material and demonstrated their efficacy in inhibiting viral replication.
Scientists at Imperial College London have developed a new method to make proteins form crystals using 'smart materials' that remember the shape and characteristics of the molecule. This technique should assist research into new medicines by helping scientists work out the structure of drug targets.
Physicists at the University of Michigan have successfully created 3D arrays of optically induced crystals using laser beams. The technique allows for the formation of crystalline structures without the need for X-ray crystallography, which is commonly used to analyze biological molecules.
Scientists have identified the molecular structure of proteins enabling bacterial cells to transfer electrical charge, opening the door to efficient microbial fuel cells. The discovery could also lead to the development of microbe-based agents for oil and uranium pollution cleanup.
Scientists at the University of Alberta discovered the first step in a bacterial immune response, where RNA is cut into pieces to target invading viruses. This finding has implications for controlling bacterial growth and fighting human infections.
Researchers discovered a strategy for disrupting bacteria's ability to communicate and coordinate virulence factor expression through compounds that bound to LuxR type receptors, rendering them inactive. This finding may lead to the development of new antibacterial therapeutics aimed at inhibiting bacterial communication.
Scientists at Duke University Medical Center have determined the structure of a nuclease that will help understand several DNA repair pathways. This discovery is important for understanding mismatch repair pathway and other pathways related to cancer biology and aging.
Rockefeller scientists have developed a new polarized microscopy technique that can help deduce the orientation of specific proteins within cells. By harnessing the unique properties of polarized light, researchers have filled in the gaps left by other techniques and made important new discoveries about protein complexes.
Antifreeze proteins have been found to bind to ice crystals through a specific mechanism involving hydrophobic and hydrophilic groups. This discovery may lead to the development of stronger, more versatile AFPs with commercial applications in various industries.
A research team led by Professor Kam-bo Wong engineered thermophilic enzymes to increase their activity at high temperatures without compromising stability. The findings provide insights into the design of biotechnologically important enzymes.
Researchers from Scripps Research Institute determine a new structure of the human A2A adenosine receptor, bound to a full agonist, revealing a super stabilizing agonist. This finding has important implications for drug design, particularly for treating diseases such as Parkinson's and COPD.
Scientists used single molecule fluorescence resonance energy transfer (FRET) techniques combined with wavelet transforms to study the AMPA receptor's behavior. They identified four distinct conformations of the receptor and found that its 'cleft' is constantly opening and closing, exploring space for neurotransmitters.
Researchers at Scripps Research and UVa determine the structure of HIV's protein package, also known as the capsid. The detailed description provides a roadmap for developing drugs that can disrupt its formation and prevent infection. The study uses X-ray crystallography to reveal the flexibility and mobility of the capsid's components.
Scientists have determined the structure and mechanism of a key enzyme in Staphylococcus aureus that produces cholesterol and a virulence factor. This breakthrough could lead to new cholesterol-lowering drugs and antibiotics against staph infections, as well as treatments for parasitic diseases.
Scientists have developed a technique to freeze the adrenaline receptor in one position, allowing them to determine its structure and develop new or better drugs. This breakthrough has significant prospects for medicine, particularly for treating asthma and heart disease, as well as understanding other GPCRs.
Researchers have characterized a series of bismuth citrate complexes and modeled the structure of ranitidine bismuth citrate, a medicine used to treat peptic ulcers and gastric reflux disease. The polymeric framework may serve as a 'drug carrier' for delivering other drugs in the human body.
Early and abundant HIV antibodies are ineffective in blocking infection due to their inability to recognize the virus until it has invaded a healthy cell. The study reveals that the virus creates two versions of the 'Achilles heel' that different types of antibodies need to target, making effective defense challenging.
Researchers at Brown University have discovered a couple of prime suspect genes, MqsR and MqsA, that control the formation of biofilms by regulating persister cell growth. The investigation provides a new avenue for developing novel sets of antibiotics targeting these proteins.
Researchers have discovered how an antibody binds to West Nile virus, neutralizing it by crosslinking protein molecules. This 'locking up' prevents the virus from infecting host cells, making it a potential target for vaccine development.
Using x-ray crystallography, researchers at Saint Louis University have revealed the molecular structure of the zymogen form of thrombin, a precursor to the active enzyme involved in blood clotting. This discovery provides crucial information about the activation mechanism and opens new opportunities for therapeutic intervention.
Canadian researchers have made a breakthrough in CO2 capture by identifying the exact sites where CO2 is held in a capture material. This discovery enables scientists to design better materials to capture more CO2, potentially mitigating greenhouse gas emissions from coal-burning flue stacks or unconventional natural gas reservoirs.
The Joint Center for Structural Genomics (JCSG), led by Ian A. Wilson, has made significant strides in high-throughput structural genomics, solving over 1,150 structures to date. The JCSG's pipeline has optimized every stage of the process, enabling large numbers of target proteins to be tackled simultaneously.
Researchers at the University of Missouri are using X-ray diffraction to study a unique enzyme found in the 'kissing bug' parasite and Aspergillus fumigatus fungus. The goal is to develop drugs that can inhibit the enzyme's activity, which could lead to breakthroughs in treating pulmonary diseases and Chagas disease.
Rutgers University has received a $47.5 million grant from the NIH to study protein structures and their impact on diseases. The grant supports two major programs: NESG, which develops new methods for determining protein structures, and SBKB, which collects and disseminates protein structure information worldwide.
A research team led by Edward Yu has discovered the crystal structures of pumps that remove heavy metal toxins from bacteria, allowing them to resist antibiotics. This finding provides a better understanding of bacterial resistance and could help drug researchers develop treatments to combat it.