Articles tagged with Protein Stability
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Researchers have identified a new class of small molecules that boost the cell's natural recycling machinery to destroy an immune-modulating enzyme called IDO1. This approach takes a bolder approach than traditional drug design, eliminating disease-causing proteins altogether and opening up new possibilities for cancer treatment.
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 discovered that disordered regions enhance specific RNA interactions in FUS protein-RNA complexes, revealing a breakthrough strategy for nucleic acid binding. The study suggests that intrinsically disordered regions actively contribute to the RNA-binding mechanism.
Researchers found that a single amino acid substitution in the ADSL enzyme affects its stability and expression, contributing to modern human differences in behavior. The study suggests that this change may have provided an evolutionary advantage in certain tasks.
Researchers found that protein structures are more like Lego than Jenga, with only a few critical amino acids in the core. A machine-learning algorithm created a tool to predict protein stability, potentially speeding up the development of new medicines and enzymes.
Researchers have developed a new protocol to exclusively access and quantify proteins carried by extracellular vesicles in the blood. This breakthrough may lead to early diagnosis of Parkinson's disease and other brain disorders, providing treatment opportunities before symptoms appear.
A recent study published in Cell reveals that nearly one in six disease-causing mutations leads to proteins mislocalizing within the cell. The research team developed a high-throughput imaging platform to assess protein location and found that breakdowns in protein stability are a major driver of misplaced proteins.
Researchers at UT Austin developed AI model EvoRank to design protein-based therapies and vaccines by leveraging nature's evolutionary processes. The model identifies useful mutations in proteins, offering a new approach to biomedical research and biotechnology.
Researchers discovered that mutations affect protein stability following surprisingly simple rules, making it possible to predict protein behavior without complex models. This breakthrough has significant implications for accelerating new treatments and designing more stable proteins with industrial applications.
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 identify UBE2J1's role in degrading the androgen receptor, a key player in prostate cancer progression. The study suggests targeting this ubiquitination machinery may help overcome antiandrogen resistance in cancer therapy.
Researchers at the University of Toronto and Sinai Health have created a new platform to identify proteins that can be co-opted to control the stability of other proteins. The study identified over 600 new effector proteins that could be used therapeutically, including those that can efficiently degrade or stabilize target proteins.
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.
Researchers investigate MCL-1i-induced Mcl-1 protein accumulation and its implications in B-cell malignancies. The study reveals a complex mechanism contributing to MCL-1 protein stability upon treatment with MCL-1 inhibitors.
Researchers identified USP7 as a novel cyclin F-interacting protein that stabilizes cyclin F protein. The study also found that USP7 regulates cyclin F mRNA, with pharmacological inhibition resulting in downregulation of cyclin F mRNA.
Researchers at Kyoto University have discovered a phosphorylation pathway that regulates meiotic double-strand break activity, ensuring genome stability. Enzymes ATR kinase and PP4 phosphatase work together to maintain a balance of DNA breaks, allowing for successful meiosis.
Research from Anglia Ruskin University found that microbial instability in the gut hinders endurance athlete performance. High-carbohydrate diets were associated with improved time trial performance, while a short-term high-protein diet led to reduced time trial performance by 23.3%.
Researchers at Hokkaido University identified two deubiquitinating enzymes, UBP12 and UBP13, that stabilize the brassinosteroid receptor BRI1 in plant cells. This finding reveals a crucial role for these enzymes in regulating plant growth and development.
The study reveals that ZNG1 is a protein that puts zinc into other 'client' proteins, playing a crucial role in regulating cellular zinc homeostasis. ZNG1's identification opens up a new area of biology for exploration and may be one of the most important regulatory strategies by which humans cope with severe zinc starvation.
Scientists have developed a proof-of-concept system that uses proteins to create stable, quantum-scale logic circuits. The circuits utilize electron tunneling behavior to modulate current and operate in a stable regime, making them suitable for high-frequency applications.
Researchers at Karolinska Institutet have found a way to stabilize the cancer-suppressing protein p53 by adding a spider silk protein, creating a more potent variant. This discovery has potential as an approach for cancer therapy.
A UC Riverside-led team developed a theory and performed simulations to understand how viruses package their genetic material. The research reveals that capsid proteins are inclined to form shells around viral RNAs due to lower stress distribution, which can aid in designing nanocontainers for drug delivery.
A study by Arizona State University shows that certain proteins can act as efficient electrical conductors, outperforming DNA-based nanowires in conductance. The protein nanowires display better performance over long distances, enabling potential applications for medical sensing and diagnostics.
A team of researchers from Tokyo Tech has identified intrinsic regulatory mechanisms that enable nascent polypeptides to stabilize ribosomes and maintain uninterrupted translation. This discovery highlights the importance of peptide sequences in regulating protein synthesis.
A team of experts from Tel Aviv University has identified 5 coronavirus proteins responsible for damaging blood vessels. The researchers hope that the identification will lead to the development of targeted drugs that reduce vascular damage in COVID-19 patients.
A digital tool developed by UK University of Bath predicts protein stability with speed and accuracy, cutting down on time and cost of drug development. The tool, called Quantitative Understanding of Bio-molecular Edge-Shift (QUBES), uses fluorescence and mathematical algorithms to analyze protein structure and predict stability.
The study used thermal proteome profiling to analyze SARS-CoV-2 infection's impact on human proteins. Hundreds of cellular proteins showed changes in abundance and thermal stability, suggesting the virus hijacks them for replication.
Researchers discovered that backbone structure is key to lab-made protein thermostability, contradicting earlier assumptions about hydrophobic core packing. This breakthrough opens doors to designing even more stable proteins for various industries.
Researchers at Tokyo Medical and Dental University and Harvard Medical School found that controlling the nuclear localization of PD-L1 can enhance the efficacy of immunotherapy for cancer treatment. They discovered that removal of a specific modification allows PD-L1 to enter the nucleus and regulate the immune response.
A research team has discovered a new mechanism for balancing protein stability during neuronal development, using heat shock proteins to regulate microtubule stability and axonal growth. This discovery can help understand neurodevelopmental diseases, nerve regeneration, and neurodegenerative diseases.
Researchers successfully used deep-sea osmolyte trimethylamine N-oxide (TMAO) to control biomolecular machines over a wide temperature range. TMAO suppresses thermal denaturation of kinesins in a concentration-dependent manner, allowing them to propel microtubules for a prolonged time.
Researchers used NMR spectroscopy and hydrostatic pressure to study the impact of internal cavities on protein stability. They found that filling these cavities with water destabilizes the protein, which has significant implications for industrial enzymes and biological drugs.
Researchers found that exposure to BMAA, a toxin produced by algae, can alter the structure of protein SOD1, leading to neurodegenerative disease ALS. The study suggests that studying patterns of SOD1 modifications may aid in developing lifestyle and preventative interventions for sporadic ALS.
Researchers find two opposing kinases regulating circadian clock, one stabilizing key protein PER2 and the other promoting its degradation. This discovery provides new targets for treating circadian disorders.
Researchers discover a new protein called ZUFSP that plays a key role in maintaining genetic stability, which is crucial for preventing cancer and other diseases. The study highlights the potential of ZUFSP as a target for drug development, particularly in treating cancer.
Talin and α-catenin proteins unfold through stable 3-helix intermediates, enabling recruitment of other binding partners and regulating protein function.
Researchers at Johns Hopkins Medicine have identified 164 long-lasting brain proteins in mice that outlast neighboring proteins by weeks and months. These stable proteins may play a crucial role in governing long-term memory and learning, as well as loss of memory, in all mammals, including humans.
Researchers have found that chaperones actively maintain proteins in a non-equilibrium but transiently stable state, even when thermodynamically unstable. This discovery challenges the long-held view that evolution has optimized protein function for thermodynamic stability.
Researchers from Jena University successfully created protein nanofibres with defined properties by combining two different proteins through a self-assembly process. The hybrid fibres can be used as components in biosensors, drug delivery particles, optical probes, or bone cements.
The protein Trigger factor recognizes a partner with unstable domains to form a stable protein duo. Chaperones like TF help folding of other proteins.
The study used FReI to investigate the folding stability and dynamics of proteins in hydrogels, revealing that hydrogels increase protein stability, speed up folding relaxation, and promote irreversible binding. The findings suggest that proteins may be destabilized when interacting with hydrogels.
Researchers linked mechanical properties of titin to animal size, revealing that larger animals had less stable proteins. By comparing ancestral protein sequences with fossil records, they estimated the weight of ancient mammals, birds, and tetrapods, finding them to be relatively small.
The study reveals that Echinolittorina snails have a unique enzyme structure that enables them to maintain protein stability at high temperatures, allowing them to thrive in hot environments. The researchers found that subtle differences in amino acid sequences between the snail proteins enabled them to remain functional and stable at ...
A team of researchers led by Paola Picotti found that only a small fraction of key proteins denature at high temperatures, contradicting previous assumptions. This discovery has implications for understanding protein stability and potentially improving the performance of heat-resistant bacteria for industrial processes.
A new study has discovered a novel route to improve the stability of protein drugs, significantly extending their shelf life. Stability increases from 14 hours to over 100 days while maintaining activity under stressed conditions, offering potential treatment solutions for diseases in developing countries.
Researchers at Duke University and NIEHS discover that dust mite allergens are both more abundant and stable than non-allergenic proteins, which may lead to new allergy treatments or predict allergenic potential of artificially added proteins. This discovery could also help characterize disease states and study drug mode-of-action.
A NIH/National Institute of Environmental Health Sciences study found that dust mite allergens are more stable and abundant than other dust mite proteins. This discovery may lead to the development of new approaches for treating dust mite allergies, a common trigger for asthma.
Scientists have discovered a way to create BioLEDs using luminescent proteins in rubber, producing white light at a lower cost and with greater stability than traditional LEDs. The technology has the potential to replace expensive and scarce materials used in white LEDs.
The researchers created a protein that can withstand various physiological and environmental conditions, allowing for more stable and effective treatments. This breakthrough could lead to advancements in biosensors and personalized therapeutics.
Researchers found that genetic mutations accepted by evolution are contingent upon previous mutations, making predictions of long-term evolution challenging. The study also revealed that mutations become entrenched and increasingly difficult to revert over time, supporting the idea that evolution is unpredictable and irreversible.
Researchers at Dartmouth's Geisel School of Medicine have identified a determinant of the circadian clock's period, suggesting that protein structure plays a crucial role in determining clock speed. This finding may lead to new treatments for sleep disorders and other health problems tied to circadian rhythms.
Researchers at NIST discover two environments for molecules in liquids and glasses, shedding light on molecular-level processes that affect protein stability. The findings provide a theoretical foundation for designing optimal sugar coatings to preserve proteins' structure intact.
Researchers at HZB's BESSY II have discovered a new class of materials using protein crystalline frameworks, which can achieve high stability and be intricately interconnected. The discovery allows for controllable interpenetration and variability, opening up potential applications.
A $1.7 million grant from NSF supports Rensselaer researcher George Makhatadze in investigating protein folding speed to expand enzymatic range for paper manufacturing and other industries. The goal is to slow protein deterioration, extending functional life at high temperatures.
Rhomboid proteases, involved in Parkinson's disease and parasite infections, are extremely slow and show no attraction to proteins, making it difficult to design drugs. These enzymes 'stop and frisk' all unstable proteins indiscriminately, allowing stable proteins to escape without injury.
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.
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.
Researchers studied model cavity and tunnel structures resembling protein binding sites to understand their ability to stay dry. Geometric shields prevent water molecules from penetrating at the nanoscale.
Whitehead Institute scientists have developed a novel method using the enzyme sortase A to site-specifically modify proteins, increasing their potency, thermal stability, and metabolism. This technique can be applied to improve therapeutically important proteins such as interferon alpha 2 and granulocyte colony-stimulating factor 3.