Articles tagged with Protein Folding
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Researchers at Colorado State University used AI to modify antibodies into stable intrabodies that can visualize histone modifications in real-time. This allows for better understanding of gene expression and its relationship with cancer and other disorders. The team created 19 new antibody-based probes with a 70% success rate, signifi...
In a new study, Northwestern scientists identified a previously unknown toxic sub-species of amyloid beta oligomers that drive brain changes in Alzheimer's disease. NU-9 decreased this toxin and reduced damage in a mouse model, suggesting it could prevent or delay the cascade of toxic events that destroy neurons.
A new study found that proteins containing a widespread structural motif are more likely to misfold in E. coli. Essential proteins with the motif are more likely to be rescued by chaperones, suggesting an evolutionary mechanism to repair them.
Researchers at MD Anderson have discovered bacterial genetic and cellular elements within brain tumor cells, potentially influencing tumor behavior. Inflammation may also drive the earliest stages of lung cancer, with targeting proinflammatory pathways emerging as a potential early intervention approach
Researchers have discovered a new class of BRCA1 mutations that can be targeted by HSP90 inhibitors, potentially improving treatment outcomes for patients with breast cancer. The study found that these mutations are more resistant to PARP inhibitor treatment but can be overcome with low-dose HSP90 inhibition.
A new mathematical framework, STIV, can predict larger-scale effects like proteins unfolding and crystals forming without costly simulations or experiments. The framework solves a 40-year-old problem in phase-field modeling, allowing for the design of smarter medicines and materials.
Researchers designed proteins with autonomous decision-making capabilities, controlling their localization based on environmental cues. This breakthrough enables more finely targeted drug delivery, reducing off-target effects and improving therapy efficacy.
A team of researchers developed a computational method that can design intrinsically disordered proteins with desired properties. The work uses automatic differentiation to optimize protein sequences and leverages molecular dynamics simulations for precision. This breakthrough has the potential to reveal new insights into diseases like...
Researchers at the University of Bath develop a peptide fragment that locks alpha-synuclein into its healthy shape, blocking toxic clumps that cause nerve cell death. The breakthrough demonstrates the potential of rational peptide design to transform large proteins into compact drug-like molecules.
Researchers identify three primary UPR pathways and their downstream cascades, which play a crucial role in the differentiation of osteoblasts and osteoclasts. Targeting these pathways with emerging drugs may alleviate bone-related events and kill tumors localized in bones.
Researchers from the Stowers Institute for Medical Research have identified a common process that powers the creation of protein formations that assemble like a 3D puzzle, triggering inflammation and cell death. This 'Catch-22' mechanism may be one of the fundamental reasons why we age.
Researchers at EPFL developed BindCraft, an open-source AI platform that uses AlphaFold2 to generate novel binders with desired functional properties. The platform reduces the need for high-throughput screening and makes protein design more democratized.
Tiny folding factories, composed of multiple chaperones, enable efficient protein folding in cells. This discovery has significant implications for treating diseases caused by misfolded proteins, such as diabetes and neurodegenerative disorders.
Researchers at Penn State have simulated a new class of protein misfolding using atomic-scale models, revealing a type of entanglement that disrupts protein function and persists in cells. The findings support the existence of this long-lasting type of misfolding, which is thought to contribute to aging and disease.
A Johns Hopkins study identifies over 200 types of misfolded proteins associated with age-related cognitive decline in rats. The findings suggest that these proteins may contribute to Alzheimer's and dementia beyond just the previously known A-beta and tau amyloids.
Daniel Hebert's life's work details how carbohydrate-related chaperones direct the protein folding process and guide proteins to their ultimate locations. The study highlights the crucial role of N-glycans in tagging misfolded proteins for destruction or correction.
Researchers have uncovered the mechanism by which ATP enters the endoplasmic reticulum, a process crucial for cellular function. The study reveals SLC35B1 as the key transporter protein, providing a promising target for therapeutic intervention.
Researchers trained AI to predict protein clumping linked to 50 human diseases. The new tool, CANYA, revealed specific chemical patterns driving or preventing harmful protein folding.
Researchers develop a simplified model of tau protein that forms disease-like fibrils, shedding light on the fundamental interactions underlying neurodegenerative diseases. The 'mini prion' can recreate the critical hallmarks of tauopathies, such as Alzheimer's disease.
The Protein Society recognizes five award winners in 2025 for their groundbreaking research in protein science and technology. Professor Jan Steyaert receives the Christian B. Anfinsen Award for pioneering nanobody technology, while Dr. Brian Kuhlman wins the Emil Thomas Kaiser Award for novel protein design and structural modeling.
Jessica Lusty Beech wins award for understanding plastic-degrading Rieske iron oxidoreductase system, while Matteo Cagiada predicts absolute protein folding stability using generative models. The Protein Society recognizes their contributions to protein science.
Researchers discovered a potential protein misfolding mechanism that could help explain unusual refolding behavior in some proteins. The team found that a type of misfolding, called non-covalent lasso entanglement, can create a barrier to the normal folding process.
A new paper proposes that temperature plays a fundamental role in setting off shapeshifting in metamorphic proteins. Researchers analyzed differences in hydrophobic contacts and found significant temperature-dependent changes, supporting their theory.
Researchers have developed new models to explore the role of a membrane anchor on the folding and aggregation of PrP. Anchoring stabilizes folding and inhibits aggregation, with clumping induced by pre-formed aggregates, suggesting a potential mechanism for infectious prion diseases.
Ana Pombo, a biochemist at the Max Delbruck Center, has been awarded the prestigious Leibniz Prize for her pioneering research on the three-dimensional structure of genomes. Her work aims to understand how environmental factors influence gene regulation and diseases like autism or epilepsy.
Researchers have discovered a mechanism to detach and recycle parts of cellular canal membranes as needed. The study, conducted with supercomputer simulations, shows that protein regions can cause the membrane to bulge and pinch off, forming vesicles for recycling.
Researchers at Linköping University have developed a new version of AlphaFold that can predict the shape of very large and complex protein structures, integrating experimental data. This breakthrough aims to improve the development of new proteins for medical drugs.
A team of researchers has identified a genetic link between rare brain malformations and protein folding defects in children. The study found that specific genetic changes can affect the function of proteins within cells, leading to abnormal cell behavior.
Scientists have developed a new class of compliant DNA nanopores that can transport molecules through cell membranes and adjust their diameter. These pores offer possibilities for biomedical applications, including targeted drug delivery and molecular diagnostics.
Scientists used artificial intelligence and molecular dynamics simulations to understand how enzymes fold lasso peptides into a unique structure. They identified key residues important for interaction with the substrate, enabling the design of new cyclase variants that can produce potent lasso peptides.
Researchers developed a cylindrical model called REMM to replicate both inner diameters and chemical properties of ribosome tunnels. The model outperformed a conventional carbon nanotube model in accurately reproducing experimentally observed protein structures.
Researchers used AlphaFold2 to predict structural effects of mutations on protein stability, finding correlations between small structural changes and stability changes. This breakthrough opens up new possibilities for protein engineering, enabling scientists to design proteins with specific functions more effectively.
Researchers have discovered that ribosomes play a crucial role in protein folding, directing folding pathways by impacting energy and stability. This discovery reveals the structural basis of how ribosomes affect protein folding, offering new insights into diseases such as cancers.
Researchers found that folded peptides are more electrically conductive than their unfolded counterparts due to the formation of a specific secondary structure called the 3_10 helix. This discovery has implications for the design and development of molecular electronic devices.
Cancer cells can attach themselves to liver cells when specific proteins are present, allowing them to colonize and form new tumors. This discovery provides insights into the metastatic process and may lead to potential treatments that prevent cancer from establishing new tumors.
Researchers at U of T have developed a deep-learning model called PepFlow that can predict the full range of conformations for peptides, which are shorter than proteins but perform similar biological functions. The model combines machine learning and physics to capture precise and accurate conformations within minutes.
Cleveland Clinic and IBM researchers develop a hybrid framework combining quantum and classical computing methods for protein structure prediction. This approach overcomes limitations of current classical methods and demonstrates improved accuracy in predicting protein structures.
Researchers use data sonification to convert molecular data into sounds, revealing how hydrogen bonds contribute to protein folding. The process involves complex interactions between water molecules and amino acids, with faster bonds speeding up folding and slower ones slowing it down.
Researchers at Rice University have made a groundbreaking discovery about protein evolution, revealing that pseudogenes can provide clues to the evolutionary journey of proteins. The team found that certain mutations can stabilize the folding of pseudogenes, but also disrupt their biological functions.
This year's winners include Professor Neil Kelleher, Dr. Tamir Gonen, Professor Margaret Sunde, and more, recognized for their pioneering research in top-down proteomics, membrane proteins, amyloid studies, and human health applications.
Researchers at Xi'an Jiaotong-Liverpool University developed a new method that enables the efficient production of cysteine-rich peptides and microproteins in their naturally folded 3D structure. The approach uses organic solvents to mimic nature's oxidative folding process, resulting in speeds of over 100,000 times faster than aqueous...
Researchers discovered how altered protein folding enables the evolution of robust bodies in yeast, allowing them to become as strong and tough as wood. This finding highlights the power of non-genetic mechanisms in rapid evolutionary change and underscores the importance of mapping genetic information to understand adaptive behaviors.
Chemical simulations can be sped up by resetting them, a new study from Tel Aviv University found. This technique, called stochastic resetting, overcomes the timescale problem, allowing for more accurate predictions of slow processes.
Researchers have provided new details on structures resulting from 3D domain swapping in antibody light chains, shedding light on mechanisms of protein aggregation. The study suggests that the formation of tetramers may prevent protein aggregation by decreasing flexibility.
A team of researchers at UMass Amherst has discovered a crucial role played by the enzyme UGGT in protein folding. The study reveals how UGGT 'tags' misfolded proteins with specific sugars, enabling chaperones to identify and correct errors.
A new MIT study proposes a theoretical model that helps explain how cells maintain the memory of their cell type despite losing chemical modifications during DNA replication. The research team suggests that the 3D folding pattern of the genome determines which parts will be marked by these chemical modifications.
The A3D-MOBD is a comprehensive database for studying protein aggregation in twelve model organisms. It contains over half a million predictions of protein regions prone to forming aggregates, providing insights into the basis of this phenomenon.
Researchers used molecular dynamics simulations to study how urea and alcohol induce structural changes in proteins, with a focus on stabilizing helices and coils. The team identified preferential binding parameters for both cosolvents, demonstrating opposing effects that can be predicted using computational methods.
A new study doubles the number of protein families known up until now and identifies many novel structure predictions using a massive analysis of 1.3 billion proteins. The researchers leveraged AI methodologies to unravel the roles of previously unknown protein sequences, expanding the horizons of potential functions.
Researchers have discovered a peptide that stabilizes the normal structure of alpha-synuclein protein, preventing misfolding and toxic clumps. This breakthrough could lead to new therapeutic developments for neurodegenerative diseases like Parkinson's.
Researchers used AI to predict 3D shapes of over 215 million proteins, providing insights into their functions and evolution. The Protein Universe Atlas offers a valuable resource for scientists to explore protein diversity.
Researchers at Aarhus University have unraveled the mystery of how lipid layers on cell surfaces accelerate Parkinson's disease misfolding. The study reveals that elevated concentrations cause alpha-synuclein to adopt an upright conformation, leading to easier refolding into dangerous aggregates.
A team of scientists from Seoul National University, ETH Zurich, and EMBL-EBI have developed a method to compare the shapes and structures of hundreds of millions of proteins. This approach has led to the discovery of unexpected similarities between human proteins involved in the immune system and proteins found in bacteria. The findin...
Researchers found that AvrE/DspE family proteins, used by plant pathogens to cause disease, fold into a straw-like structure with a water channel. This discovery could lead to the development of new methods to disarm these proteins and prevent crop damage.
A Kyoto University team reveals the Dumpy protein as the key factor in controlling 3D tissue structures through external cues. This finding challenges traditional understanding of morphogenesis and opens up new avenues for manufacturing controllable 3D tissue folding with coordinated cell behaviors.
Complex proteins adopt multiple structural states in solution, making it challenging to determine their three-dimensional structure. A new approach combining NMR spectroscopy and computer simulations reveals the dynamic properties of these proteins.
Researchers from the University of Kansas have created a powerful dataset to facilitate drug development against gram-negative bacteria. The dataset reveals over 270,000 previously unidentified outer-membrane proteins with potential as vaccine targets.
Researchers have created self-assembling protein-mimics that can selectivity transport water across membranes while rejecting salts, offering a potential solution to improve energy efficiency in industrial water purification. The oligourea foldamers are smaller and more stable than existing artificial water channels.
A new study reveals that the cellular chaperone protein GRP78 migrates to the nucleus under stress and alters gene activities, allowing cancer cells to become more mobile and invasive. This discovery offers potential new approaches for cancer treatment, including down-regulating GRP78 activity or preventing it from binding to ID2.
Researchers developed a new high-throughput approach to evaluate protein folding stability, identifying factors contributing to stability and informing predictive models. The cDNA display proteolysis method permits large-scale analysis of nearly 900,000 proteins, shedding light on diseases involving misfolded proteins.