Articles tagged with Protein Structure
A new study analyzed dynamical properties in antibiotic resistance enzyme β-lactamase, finding significant evolution across bacterial families without limiting new antibiotic resistance. Minor changes in the enzyme's active site can adapt it to new antibiotics.
Researchers visualized ER sheet stacking revealing a 'parking garage' structure with helical ramps for efficient protein synthesis. This optimized structure allows for maximum space usage within cells.
Researchers have captured a key step in the molecular 'dance' necessary for cell division by imaging the enzyme that unwinds DNA double helices. The study reveals how this enzyme recruits and interacts with the origin recognition complex, enhancing understanding of essential biological processes.
Researchers have identified a unique protein structure in the chlamydia bug that could lead to novel diagnostic methods and treatments. The discovery may help combat this sexually transmitted disease, which affects an estimated 2.8 million people in the US each year.
McGill University researchers have discovered the three-dimensional structure of the Parkin protein, which protects neurons from cell death due to damaged mitochondria. The study's findings suggest that designing mutations in Parkin could provide better protection for nerve cells and potentially slow disease progression.
Researchers have discovered a target for Schmallenberg virus treatment by identifying the nucleocapsid protein as a key building block that can be blocked to kill the virus. The study, published in Nucleic Acids Research, provides insight into the structure and function of the protein.
Researchers determined the three-dimensional structure of a protein pair, LC8 and Nek9, which plays a crucial role in cell division. This discovery has implications for studying diseases related to cell division processes like cancer.
Scientists have long debated the structure of alpha synuclein, a protein associated with Parkinson's. A new study models its structure, finding that it can rapidly switch between different conformations. The researchers suggest that stabilizing an ordered structure could prevent aggregation and offer a new drug-design strategy.
Researchers have successfully studied the shape of proteins using a novel strategy combining computational modeling and experimental techniques. This breakthrough has implications for understanding protein functions and diseases such as cancer, Parkinson's, and Alzheimer's.
Researchers mapped protein structures and organisms onto a timeline, revealing an 'hourglass' pattern where proteins folded faster over time. This discovery sheds light on the evolutionary drivers behind protein folding and has implications for understanding molecular functions, genetic engineering, and synthetic biology.
Researchers at CNIO have developed new computational methods to study the evolution of proteins and their interactions. These methods enable predictions of molecular relationships and structural changes, with potential applications in cancer treatment and drug development.
A study by HITS researchers found that most proteins evolved to fold faster, with a 'big bang' of complex structures emerging 1.5 billion years ago. The study suggests that faster folding speeds may make proteins less susceptible to aggregation.
Researchers at the University of Minnesota created an artificial enzyme through directed evolution, a method that mimics natural selection and evolution. The new enzyme functions similarly to its natural counterparts despite its unusual structure and dynamics.
Researchers at the University of Illinois have made a groundbreaking discovery in the study of enterococcal cytolysin, a 'virulence factor' that kills human cells. The enzyme responsible for its formation was found to produce distinctly different ring structures with unusual stereochemistries.
Researchers at TSRI have determined the structure of Ltn1, a 'quality-control' protein that ensures protein-making machinery works smoothly. The study suggests Ltn1 may be relevant to human neurodegenerative diseases such as ALS.
Intrinsically disordered proteins (IDPs) may still have functions without a rigid structure, while protein flexibility is crucial in molecular recognition. The debate highlights the complexity of protein behavior and the need for experiments to determine the true nature of protein recognition.
Researchers develop principles to generate ideal protein structures by consistently favoring specific folding patterns. This allows for the creation of robust and stable building blocks for engineered functional proteins, which could be useful in drug development, vaccine creation, and industrial applications.
Researchers at Johns Hopkins Medicine found that the location of rhomboid proteases within membranes enables them to recognize and cut unstable proteins. This discovery has profound implications for understanding diseases like Alzheimer's and developing treatments.
Researchers at Berkeley Lab discovered that protein-folding funnels can also apply to self-assembly of multiple proteins. The findings provide important guidelines for future biomimicry efforts, particularly in device fabrication and nanoscale synthesis.
Research reveals that the amount of protein in solution determines the formation of fibrils, which can lead to cell death. Developing treatments for diseases caused by protein aggregation is a possibility with this new knowledge.
The European Drug Initiative on Channels and Transporters (EDICT) project has enabled a major step forward in understanding membrane protein structures and functions. Over 30 proteins have been studied, with at least six potential new drug compounds identified.
Researchers have identified 21 proteins that interact with ataxin-1, which can enhance or prevent its misfolding and toxicity. The study found that proteins with a specific structure called 'coiled-coil-domain' promote aggregation and toxic effects.
Researchers at Aarhus University have solved the long-standing puzzle of haemoglobin structure using high-resolution three-dimensional mapping. This discovery provides essential information on how haptoglobin captures and neutralizes toxic haemoglobin, which can cause kidney damage in diseases like malaria.
Hao Yan leads elite team to develop nano-scale devices mimicking biological systems, aiming to simplify biochemical pathways and advance biomedicine and energy research. The $6.25M award supports ASU's biomimetics and bio-inspired engineering research program.
Researchers have elucidated the structure of a key protein involved in DNA double-strand break repair. The MRN complex plays a crucial role in cell survival and function, with mutations linked to distinct syndromes and predispositions to cancer, radiation sensitivity, and neurodegeneration.
A new study finds strongly conserved parts of proteins responsible for knotted portions display remarkable similarities among species separated by more than a billion years. Slipknotted proteins, rare but essential for cell membrane stability, are also widely distributed across different families and species.
University of Montreal researchers developed a strategy to monitor protein assembly by integrating fluorescent probes throughout the linear protein chain. This approach enables capturing snapshots of protein shape at each stage of assembly, shedding light on how proteins self-assemble into working nanomachines.
A new study reveals that protein knots, a complex structure, are strongly conserved in nature, suggesting they have specific functional advantages. The researchers found that knotting patterns are highly conserved, with flexible points of entry, which may contribute to the stability and function of proteins.
Researchers have designed specialized proteins that assemble to form tiny molecular cages, which may be used for drug delivery or as artificial vaccines. The cages are hundreds of times smaller than a single cell and can be decorated with virus-identifying proteins to stimulate an immune response.
Researchers at Salk Institute create cell-free expression system to synthesize and analyze integral membrane proteins, solving their three-dimensional structures in just 18 months. This breakthrough enables precise biochemical mechanisms understanding and targets the proteins with new drugs.
Researchers at the European Molecular Biology Laboratory have discovered a 'transformer' protein that allows cells to create vesicles of different shapes and sizes by changing the shape of individual building blocks. This breakthrough provides new insights into the structure and function of COPI protein-coated vesicles.
A new research at Washington University School of Medicine has shown how an unusual protein plays a key role in temporarily blocking the movement of ions through channels after a cell fires off an electrical signal. The researchers found that this protein nestles into a receptor inside the channel in a highly specific way, closing it a...
Researchers at the University of Bristol have discovered that a protein can refold its structure in an environment devoid of water molecules. This finding has significant implications for the development of new industrial enzymes with hyper-thermal resistance.
A new solid state NMR method helps visualize protein shapes, aiding understanding of biological molecules' functions and behaviors.
Scientists have determined the molecular 3D structure of a protein in blood platelets and a receptor that controls blood clot formation. This discovery helps understand the body's response to superbugs and potentially leads to new treatments.
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.
Researchers discovered the structure of type VI secretion system apparatus and proposed how it works by firing spring-loaded molecular daggers. The nano-weapon can pierce cell membranes and inject proteins, evading detection for decades with traditional electron microscopy.
A new study by Rensselaer Polytechnic Institute researchers reveals that the size and curvature of nanosurfaces significantly impact protein orientation and stability. This discovery is crucial for controlling protein function in various biological applications, such as biosensors and tissue engineering.
Scientists have made new discoveries about the shape and structure of biological molecules, potentially leading to new treatments for neurodegenerative diseases. The research found that two protein channels are similar in structure and function, with one 'unlocking' calcium flows inside cells.
Scientists have developed a new technique that allows them to create detailed 3D images of individual proteins using cryo-electron microscopy. This breakthrough enables researchers to study the flexibility and movement of proteins, which is crucial for understanding their function and developing new drugs.
Researchers have elucidated the structure of the 26S proteasome, a key protein degradation machinery, using a combination of structural biology methods. The discovery sheds light on how cells dispose of their waste and could have important implications for understanding neurodegenerative diseases like Alzheimer's and Parkinson's.
Scientists have solved the three-dimensional structure of a newly discovered type of gene-targeting protein called TAL effector, which has a unique LEGO-like modular architecture. This discovery enables researchers to engineer the protein for targeted gene modification, genetic engineering, and corrective gene therapy.
Researchers developed a new method called HHblits that surpasses PSI-BLAST in performance by increasing sensitivity and precision. By analyzing similar sequences, scientists can infer the structure and functions of proteins more accurately and frequently than before.
A team of international researchers has developed an algorithm to infer the internal interactions of proteins and generate their atomic details from sequence information alone. This method could revolutionize the understanding of protein shapes and their functions, leading to breakthroughs in biology and medicine.
A Harvard Medical School team developed an algorithm that infers essential information about microscopic interactions in proteins using evolution and high-throughput genetic sequencing. This approach solves the computational protein folding problem, predicting accurate shapes for diverse proteins.
Researchers at Berkeley Lab create a new device called the SheetRocker to study how shaking affects sheet formation in peptoid monolayers. They find that compression on the air-water interface produces free-floating, stable nanosheets in 95% yield, enabling scalable sensing and filtration applications.
Brandeis researchers have produced and determined the structure of alpha-synuclein, a key protein linked to Parkinson's disease. The findings may lead to the development of new treatments by stabilizing the protein.
Researchers at Rutgers and UMDNJ have determined the structure of a protein that recognizes viral RNA, providing unprecedented insight into fighting viral infections. This discovery could lead to the development of broad-based drug therapies to combat viral infections such as influenza, hepatitis C, and measles.
A team of gamers solved the molecular structure of a retrovirus enzyme using online game Foldit, achieving results in just three weeks. The breakthrough could lead to the development of new anti-AIDS drugs by targeting specific features on the molecule.
The Seattle Structural Genomics Center for Infectious Disease has solved over 375 protein structures, providing a blueprint for fighting infectious disease. The center's work may lead to new drug therapies urgently needed to prevent outbreaks of multi-drug resistant and XDR strains of TB.
Researchers discover that alpha-synuclein, key to Parkinson's disease, forms complex folded tetramers in healthy cells rather than a single, randomly-coiled chain. This finding challenges existing disease paradigms and suggests a new therapeutic approach.
A Vietnamese PhD student, Tung Le, has made a breakthrough in understanding how an antibiotic-producing organism controls resistance to its own antibiotic. His research shows that the SimR protein regulates antibiotic export by binding to DNA or the antibiotic itself.
Researchers at UCI have found a new method for predicting how influenza proteins evolve, allowing for potential pharmaceutical exploitation. This approach could aid the development of new drugs targeting so-called 'flu protein pockets'.
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 the University of Pennsylvania have developed an algorithm to computationally select the best proteins for building nanostructures, drawing inspiration from biological structures. The method eliminates thousands of candidate proteins to identify suitable ones, making the protein selection process more efficient.
Scientists have solved the structure of a key malaria parasite protein that controls cell movement, overturning decades-long understanding. The discovery could lead to novel anti-malarial treatments and cancer therapies targeting actin proteins.
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.
A Kansas State University biochemist is using computer models to study the protein p21, which plays a key role in regulating cell division and has connections to cancer and aging. The study provides insights into how structural flexibility influences the function of this intrinsically disordered protein.
Researchers at the University of Leeds have uncovered the first misfold that triggers the formation of amyloid fibres, a critical step in understanding these disease-causing structures. This discovery offers new targets for therapies and may shed light on other protein-related diseases.
Researchers found that approximately 90% of protein-protein interfaces have close structural neighbors, and most interfaces are roughly planar. The study suggests that the interfaces' structures depend on simple physics principles and are primed for promiscuity, which could help explain biological phenomena and inform drug discovery.