Articles tagged with Protein Structure
Scientists at VIB discover that mutations at specific positions can suppress protein aggregation, increasing solubility. This breakthrough could enable the production of protein drugs and enzymes with improved stability and functionality.
Researchers have captured a snapshot of how coronaviruses enter cells using high-resolution cryo-electron microscopy. The atomic model suggests specific vaccine strategies against SARS-CoV and MERS-CoV. A fusion peptide on the outer edge of the spike protein may be an ideal target for neutralizing coronaviruses.
Researchers aim to uncover mechanisms that regulate plants' defence against stress factors, leading to the development of new crop species. Fluctuating protein structures may be essential for carrying out specific functions.
The study reveals the core of protein clumps found in Huntington's brains has a distinctive structure, which may lead to new therapies. The findings provide crucial insights into how proteins undergo misfolding and aggregation, shedding light on neurodegenerative diseases.
Researchers used mathematical calculations to create a complete picture of protein nanoparticle surface morphology, identifying structures most advantageous for vaccine design. This approach may lead to the development of cost-effective vaccines, including a malaria vaccine set to start clinical testing soon.
Researchers have discovered the structure of TRPV2, a protein linked to pain and heat perception, which could lead to new treatments for chronic pain. The study found that TRPV2 has an in-between state where it becomes desensitized to repeated stimuli, suggesting a potential way to alleviate chronic pain.
Researchers discovered how nucleophosmin (NPM1) transforms between two forms: a disordered monomer and a folded pentamer, influenced by phosphorylation and partner binding
Researchers at the University of Basel have solved the structure of mammalian TOR complex 1 (mTORC1), a critical regulator of cellular processes. The study reveals the unique architecture of mTORC1, highlighting the importance of partner proteins in its function.
Researchers have made significant breakthroughs in protein structure prediction and design, enabling the creation of new proteins with unprecedented accuracy. By leveraging computational design and collaborative efforts, scientists can now devise amino acid sequences that fold into novel structures, far surpassing what is predicted to ...
Research at INRS demonstrates that small changes in enzyme structure can significantly impact its function. The study reveals how the subtle dance of atoms affects enzyme activity, shedding light on protein engineering failures and improving synthetic functional enzymes.
A recent CSIRO study maps the boundaries of the 'dark proteome', a region of proteins with completely unknown structure. The research identifies surprising features in nearly half of the eukaryotic proteome, including associations with secretory tissues and disulfide bonding.
A team of scientists at Case Western Reserve University has produced the first image of a human protein binding with ribonucleic acid (RNA), shedding light on how some viruses, including HIV, replicate their genetic material. The discovery could lead to new strategies to block viral replication and limit or halt infection.
Researchers at KAIST and UCLA developed a method to manipulate membrane protein folding in a natural environment, revealing cooperative folding behavior. The study used magnetic tweezers to induce unfolding and refolding, allowing for the mapping of folding energy landscapes and kinetic rates.
A new synthesis method for glucosepane, a molecule implicated in diseases such as diabetes, has been developed by researchers. This breakthrough allows for the production of glucosepane's various forms, which may help uncover its role in health complications and potential countermeasures.
Researchers have created the first three-dimensional image of the Trib1 protein, which plays a vital role in controlling protein degradation and balancing levels in cells. This discovery could help develop new drugs to treat cancers such as acute myeloid leukaemia by blocking overproduction of Trib1.
Researchers find siderocalin protein facilitates uptake of radioactive toxic metal ions in cells, opening new avenues for remedial action. The protein's structure has been characterized, revealing a possible target for treatment strategies.
A team led by Carnegie Mellon University physicists has discovered the structure of PTEN, a key tumor-suppressing protein. The findings reveal how PTEN regulates cell growth and suppresses tumor formation through dimerization, providing new insights into cancer development and potential therapeutics.
Researchers have developed a new method for studying protein structure using nanoscopic pores, allowing for the analysis of individual proteins without modification. This technique enables the detection of protein aggregates, which are associated with diseases like Alzheimer's and Parkinson's.
Researchers at Sanford Burnham Prebys Medical Discovery Institute solved the structure of hypoxia-inducible factors (HIFs), important regulators of tumor response to low oxygen. The findings identify potential targets for new cancer drugs, which could inhibit HIF functions and reduce tumor growth.
A study at Umea University has successfully captured a protein structure previously impossible to study, providing insights into enzymes' catalytic capabilities. The discovery enables the development of designed enzymes for new chemical reactions in biotechnology.
A team from Harvard Medical School has revealed the atomic level structure of VSV polymerase protein L, a key component in RNA virus replication. This finding provides insights into how these viruses copy their genomes inside host cells.
The tool collects non-redundant PTM data across all known members of a protein family and projects it onto 3D protein structures to visualize PTM hotspots. By analyzing these hotspots, scientists can prioritize research on proteins with high potential for biological function.
A recent study has provided a more complete picture of how proteins move, laying the foundation for understanding molecular causes of human disease and developing potent drug treatments.
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 have discovered the structure of a key protein on the surface of the mimivirus, aiding efforts to determine its hosts and unknown functions. The R135 protein is similar to an enzyme found in a fungus and may participate in biodegrading lignin, suggesting alternative hosts such as algae.
A new study demonstrates the ability to visualize metabolic enzyme structures at near-atomic detail using cryo-electron microscopy. This advancement has immense implications for drug design and development, revolutionizing the field of structural biology.
Scientists have decoded the molecular basis for mitochondrial membrane folds, which allow cells to use food energy efficiently. The discovery of Mic10, a protein component, reveals its role in controlling transport and insertion into the inner membrane system of mitochondria.
Researchers developed a new computational method called AGGRESCAN3D to study protein aggregation in 3D. The algorithm surpasses limitations of previous methods and offers improved precision in predicting protein aggregation properties.
Researchers found a way to predict protein structures by breaking them into smaller fragments and analyzing their distributions in nature. This discovery could lead to understanding how certain mutations cause disease and developing new treatments.
Researchers at Iowa State University and the Ames Laboratory have discovered two proteins that pump antibiotics out of bacteria, allowing them to resist medications. The study reveals that these efflux pumps are part of a large family of proteins and may help protect cells from certain drugs.
Scientists at the University of Illinois have developed a new lab technique that simultaneously observes protein structure and function in DNA repair. The technique, combining fluorescence microscopy and optical trapping, provides definitive answers to long-debated questions and opens up new avenues for biological engineering.
Moffitt scientists developed a novel technique to analyze the MDMX protein, revealing its auto-inhibitory segment that controls p53 activity. This discovery may help identify patients more likely to respond to an MDMX-targeted cancer drug.
The molecular structure of the cytotoxin from Mycoplasma pneumoniae has been determined, which could lead to the development of effective drugs and vaccines to neutralize its injurious effects. The discovery is a significant breakthrough in understanding respiratory infections such as asthma.
A study by UCSB scientists examined the unique properties of tau, a critical protein in neurons that can form clumps associated with Alzheimer's disease. Researchers found that exposing tau to certain chemicals, such as urea, could prevent aggregation, while another compound, TMAO, accelerated it.
Researchers have developed a molecular mouse-trap technique that aids understanding of cell division and its role in cancer. By studying the structure of proteins involved in chromosome formation, scientists can develop new approaches to analyze complex biological molecules.
Researchers at UNIGE reconcile two dominant endocytosis theories, proposing a balanced interplay between clathrin proteins and other adaptors. The study suggests that clathrins do not dominate the process, but rather contribute to a subtle energy-based deformation of the membrane.
Researchers at the University of Granada have successfully modified a type of lactose protein called beta-lactoglobulin using pulsed light, making it easier to digest. The treatment facilitates digestion, particularly in the small intestine, without altering the protein's functional properties.
The Aquaria project has created a powerful web resource that simplifies the process of gleaning insight from 3D protein structures. The tool offers around 46 million computer models, allowing users to view additional information such as genetic differences mapped onto 3D structures.
Biochemists elucidate protein complex structure in the respiratory chain, a crucial process for cellular energy production. The study reveals how complex I switches between active and inactive forms, shedding light on its role in disease, including Parkinson's and myocardial infarction.
Researchers at Max Planck Institute of Molecular Physiology studied the three-dimensional structure of the ryanodine receptor using electron cryo-microscopy and a new technique for detecting electrons. The high-resolution structure reveals how the protein changes its shape upon binding calcium ions.
Researchers successfully analyzed all known complete proteomes using X-ray crystallography and homology modeling, covering 25% of protein clusters. The study highlights the potential for knowledge-based target selection to increase structural model production, particularly in eukaryotes and archaea.
Case Western Reserve researchers have identified a protein mutation that prevents proper gonadal tissue development, leading to cancer and other issues. The discovery highlights the importance of the SRY protein in regulating male sex determination and has implications for understanding birth defects and cancer.
The structure determination of a lipid scramblase reveals a novel protein architecture that enables the transport of lipids across cell membranes. The discovery provides insight into the activation of the protein by calcium and has implications for understanding previously unknown mechanisms of lipid transport.
Scientists have obtained the first high-resolution structure of HIV's immature form, revealing a surprising arrangement of its building blocks. This breakthrough enables researchers to probe further into potential drug targets and understand how mutations influence virus assembly.
Researchers at Montana State University provided the first blueprint of a bacterium's molecular machinery, showing how bacterial immune systems fight off viruses. By understanding CRISPR mechanisms, scientists can potentially develop therapies for plant, animal, and human diseases.
Researchers have developed a new method to measure structurally modified proteins in complex biological samples, enabling the analysis of thousands of proteins. The method uses a combination of digestion enzymes and Selected Reaction Monitoring to quantify protein quantities and determine structural changes.
Researchers have elucidated the atomic structures of sugar transporters, revealing an 'airlock-like' mechanism that moves sugars in multiple stages. This discovery is crucial for understanding diseases like diabetes and improving crop yields.
EPFL researchers developed a synthetic amino acid that can impact 3D structure of bioactive peptides, enhancing their potency. The amino acid, similar to cysteine, forms bridges influencing overall structure and function of peptides and proteins.
Researchers developed olive oil 'bulking agents' to replace pork fat in hot dogs, maintaining texture and reducing calories. The substitutes contain 55% olive oil, which contains more healthful unsaturated fats, making them suitable for summer BBQs.
Researchers have identified a protein that regulates calcium levels in cells, which could be a promising strategy for fighting cancers. The study reveals how this protein serves as a molecular safety valve to maintain steady calcium levels.
The Protein Data Bank has surpassed 100,000 entries, providing a wealth of structural data for researchers to understand biological mechanisms and discover new medicines. The archive's growth is driven by the efforts of structural biologists worldwide, who continue to deposit new structures and improve the resource.
The study reveals that chaperones, like GroEL and GroES, use a high-speed origami-like mechanism to accelerate protein folding. This process, which was previously thought to be energetically unfavorable, is now understood to be a favorable reaction, allowing proteins to fold faster than they are produced.
Researchers have determined the structure of a protein produced by Candida albicans, a common fungal pathogen that causes yeast infections and other diseases. The discovery could lead to the development of targeted compounds to treat widespread fungal infections.
Dr. Ira Kurtz's research aims to understand the molecular processes affecting kidney function, with a focus on designing specific drugs targeting disease-causing proteins. The goal is to reduce side effects and costs associated with current treatments, which affect millions of people worldwide.
Researchers discovered varied gene expression patterns between male and female athletes, with altered signaling pathways regulating cartilage growth. The findings suggest genetics may play a role in the higher incidence of ACL injuries among females.
SURA honors Dr. Jeffrey Skolnick, a renowned biologist at Georgia Tech, for his groundbreaking research on protein structure and function. His cutting-edge discoveries have the potential to dramatically accelerate and enhance the drug discovery process.
The Vanderbilt team has deciphered the 3-D structure of a key MRSA protein, FosB, which inactivates an antibiotic called fosfomycin. This discovery may enable the design of inhibitors that can improve the effectiveness of fosfomycin and combat MRSA infections.
Researchers have identified the first structure of one of eight human amino acid transporters, known as HATs. This breakthrough provides new insights into their functions and opens up possibilities for developing drugs to tackle various diseases associated with HATs.
Researchers at Cold Spring Harbor Laboratory have discovered two proteins that control the structure of chandelier cells, a type of inhibitory neuron important in epilepsy and schizophrenia. The study found that DOCK7 and ErbB4 regulate axonal projections, allowing one cell to block or modify hundreds of other cells.
Researchers at Duke University have determined the structure of a key part of the HIV envelope protein, gp41 membrane proximal external region (MPER), which previously eluded detailed structural description. This discovery will help focus HIV vaccine development efforts.