Researchers developed a new approach to identify protein structure from sole sequence information by analyzing paired mutations across thousands of protein family members. This method identified sequence covariations that uncover the protein's macrostructure and its fundamental structural and functional units.
A single amino acid change determines which species are vulnerable to a hereditary brain disease. The human, mouse and hamster forms of the protein have distinct three-dimensional structures at the atomic level.
Researchers at CNRS have identified a novel protein, KSRP, specific to the ribosomes of trypanosome parasites. Inhibiting its activity leads to parasite death. This discovery opens the path to developing new, safer therapies for Chagas disease and African sleeping sickness.
Exosomes secreted by cells in healthy individuals stop protein aggregation that leads to type 2 diabetes, but those in patients with the disease do not. This discovery provides new insights into the disease and may lead to the development of treatments.
Researchers from the University of Alabama at Birmingham have solved the last unknown protein structure of HIV-1, which helps understand how the virus infects human cells and assembles progeny viruses. The cytoplasmic tail of gp41 protein plays a crucial role in virus assembly and replication.
Researchers at the University of Notre Dame have developed a new analysis procedure to better understand how intrinsically disordered proteins (IDPs) function in cells. The study finds that most IDPs are more disordered than previously thought, which could lead to new strategies for preventing protein misfolding diseases.
Researchers at the University of Dundee have identified the 3D structure and inner workings of the PINK1 enzyme, a key player in protecting brain cells against stress. This breakthrough provides crucial insights into how PINK1 exerts its protective role in Parkinson's disease.
The 2017 Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for developing cryo-electron microscopy. This technology allows researchers to freeze biomolecules mid-movement and define protein structures at atomic resolution.
Researchers developed a theoretical method to calculate biomolecule conformations and demonstrate consistency with experimental results. The model sheds light on the role of amino acid structures in protein functions, revealing potential for extrapolating properties to larger systems.
Researchers from MSU have discovered a novel mechanism of carotenoid transfer between two proteins, opening doors for the development of water-soluble protein complexes to deliver antioxidants to cells. This discovery may lead to new therapeutic applications, such as protecting healthy tissue during cancer treatment.
Researchers created three-dimensional structures that mimic natural enzymes, shedding light on folding processes and potential treatments for diseases like Alzheimer's and Parkinson's. The breakthrough allows for the analysis of misfolded proteins, a key factor in these conditions.
Researchers stopped FUS protein clumping using phosphorylation, a natural cellular process that increases protein charge and repels aggregation. The findings could have positive implications for treating ALS and dementia.
The Rice lab has produced the first full-length structure of a salmon virus protein, shedding light on its role in viral assembly and potentially informing strategies to treat human influenza viruses. The discovery could lead to new antiviral treatments by targeting the protein's interaction with other viral components.
A new tilted microscopy technique reveals better protein structures, resolving missing information and improving disease research. This approach could lead to a deeper understanding of proteins' conformations and their role in various diseases.
Researchers from the Bristol BioDesign Institute created a miniprotein with a stripped-down structure to investigate molecular forces that assemble and stabilize protein structures. They discovered subtle forces beyond hydrophobic interactions, which could lead to new drug targets.
A Los Alamos research team used neutron crystallography to determine the three-dimensional structure of a protein that breaks down cellulose, a key step in creating biofuels. The findings suggest that understanding the mechanism of this enzyme could lead to more efficient and cost-effective production of ethanol.
Research in The FASEB Journal reveals a key role for cilia structure in determining susceptibility to neural tube defects. Genetically modified mice studies found that methylation of the Septin2 protein affects neural tube closure, leading to an increased risk of birth defects.
A team of researchers at Hokkaido University has uncovered the structure of a protein called HLA-G2 that protects embryos from being attacked by their mothers' immune systems during pregnancy. The structure was found to be similar to another class of human leukocyte antigens, suggesting its evolutionary origin.
An international team of scientists has determined the 3-D atomic structure of over 1,000 proteins that are potential drug and vaccine targets. The experimentally determined structures have been deposited into the World-Wide Protein Data Bank, freely available to the scientific community.
The team developed a new chemical tool to reveal the topology of IMM proteins in live cells, confirming 58 topologies and determining 77 previously uncharacterized ones. This breakthrough will help speed the development of mitochondria-targeted therapeutics for various human metabolic diseases.
A recent study from Indiana University found that tiny changes in protein atom movement can significantly impact bacterial function and evolution. Researchers discovered that atomic motions play a major role in controlling protein activity, allowing bacteria to rapidly evolve new ways to overcome medical treatment.
The 2017 winners of the Protein Society Awards include Dr. Billy Hudson, Dr. Lewis Kay, Dr. Juli Feigon, and others who were recognized for their groundbreaking research in protein science.
A recent study by Indiana University researchers has mapped a key protein of the Zika virus, enabling the analysis of existing drugs and compounds that can disrupt its spread. The study's findings offer hope for finding effective treatments against the disease, which causes birth defects and neurological disorders in infants and adults.
Researchers at Karlsruhe Institute of Technology developed a method to predict protein structures using statistical analyses. This approach allows for the prediction of even complex protein structures without experimental determination, potentially leading to new treatments for diseases like Alzheimer's.
Researchers at TUM have developed a method to construct custom DNA-protein hybrid structures using genetically encoded proteins and DNA. This approach allows for the creation of complex shapes and spatial arrangements that can be used to investigate fundamental processes in cell biology and biotechnology.
Researchers have characterized the structure of a protein from sand flies that can convey immunity to Leishmania parasites. The SALO protein showed promise in inducing long-term protection against leishmaniasis in mice, with no appreciable similarities to human proteins.
Biophysicists at JILA measured protein folding with unprecedented detail, identifying 14 intermediate states in bacteriorhodopsin. The discovery reveals previously unknown dynamics, shedding light on the complex behavior of membrane proteins.
EHD proteins assemble on the surface of cells to create vesicles, which are used to transport molecules and transmit neural signals. The molecular machines reorganize membrane structure through ring-like formations.
EPFL scientists developed a new computer model to predict allosteric pathways for enzymes and other proteins, enabling more efficient drug design. The model proposes a new hypothesis for allosteric architectures, introducing the concept of 'levers' that amplify responses at a distance.
Scientists accurately predict protein volume changes upon unfolding, resolving a long-standing paradox. The new method, developed by Rensselaer Polytechnic Institute researchers, reveals that unfolded proteins gain and lose volume in intricate ways.
University of Toronto scientists have discovered a better way to extract proteins from membranes, making it easier to study cell communication and human health/disease. Using a type of polymer, they stabilized proteins while keeping fatty molecules attached.
Researchers developed machine learning algorithms to reconstruct 3D protein structures using microscopic images, enabling faster discovery of new drugs for diseases like Alzheimer's and cancer. The approach eliminates prior knowledge requirements, making it possible to study previously inaccessible proteins.
Researchers have engineered biomimetic structures from mysterious class of disordered proteins, enabling controlled self-assembly and disassembly. This breakthrough will facilitate thorough studies of these proteins and their cellular function, leading to new opportunities for biomedical applications.
Researchers have made a groundbreaking discovery by directly observing the structure of protein machinery in living cells, allowing them to study its functions in unprecedented detail. This breakthrough has significant implications for understanding cellular biology and developing new therapeutic strategies for diseases.
Researchers created the first three-dimensional map of the cystic fibrosis protein, revealing a vulnerable spot in the protein responsible for many cases of the disease. The map shows that one half of the channel bears more disease-causing mutations, including one responsible for 70% of disease cases.
Researchers at the CNIC have defined the molecular organization underlying energy production in living cells. The discovery sheds light on the regulation of metabolism and reveals a new understanding of the mitochondrial electron transport chain's structure and function.
Researchers transform protein data into musical sounds, called sonifications, to reveal insights into their structures and functions. By analyzing these melodies, scientists can identify anomalies and gain a better understanding of protein behavior.
Researchers at ETH Zurich successfully assembled protein-like structures from four simple amino acids, suggesting that these molecules may have been the precursors of life. The findings support the 'amyloid hypothesis,' which proposes that ancient RNA molecules were not capable of self-replication.
Researchers have discovered that prion proteins, previously known for causing fatal diseases, may also transmit beneficial traits from cell to cell. These intrinsically disordered proteins can adapt yeast cells to stressful environments and are conserved over millions of years in human cognates.
Scientists at the University of Alberta have identified the structure of the infectious prion protein, a misfolded protein causing BSE, Chronic Wasting Disease, and Creutzfeldt-Jakob Disease. The breakthrough study uses electron cryomicroscopy technology to reveal how infectious prions replicate and propagate.
Researchers have found that p53 is more prone to aggregation than its cousins due to exposed backbone hydrogen bonds. This instability can lead to the formation of amyloid fibrils, which are associated with various cancers. The study provides new insights into p53 stability and offers potential strategies for developing cancer therapies.
Researchers have determined the detailed structure of Mitochondrial Complex I, the first and largest complex in the respiratory chain. This breakthrough allows for a deeper understanding of its intricate arrangements and interactions, enabling insights into disease-causing mutations and affected enzyme activity.
Scientists at Scripps Research Institute have determined a previously unknown structure of proteins key to making terpenoids, a family of molecules encompassing successful cancer treatments. The study provides insight into how Nature makes these compounds and may lead to engineering structural diversity in bacteria.
Scientists have discovered the molecular structure of a key Zika virus protein, shedding light on its role in viral reproduction and immune system interaction. The study provides new insights into the NS1 protein's functions and potential targets for vaccine development.
Biologists have developed an algorithm predicting protein cluster structure, enabling faster understanding of cellular functions and potential treatments. The new method is up to 100 times faster than previous methods, taking just 15 minutes to run on a personal computer.
Researchers have used molecular dynamics simulations to study the spatial and temporal behavior of myoglobin, a protein involved in oxygen transport. The simulations provide insights into the underlying chemical structure and dynamics of metastable intermediates, shedding light on the protein's function.
Researchers used a high-intensity X-ray pump/X-ray probe technique to study molecular dynamics, enabling the observation of atomic-level changes in molecules when bombarded with X-rays. This new method has potential applications in understanding light-sensitive molecules and developing novel materials for energy harvesting.
Researchers have identified essential aspects of the regulation of the anti-tumor protein p53, with surprising results suggesting that only a few ribosomal proteins are required to maintain nucleolar structure. This discovery has significant implications for cancer research and development of new biomarkers.
By combining FTIR spectroscopy with microarrays, researchers can extract detailed information about protein structures and bonding, allowing for precise quantification and analysis of proteins in minute amounts. This breakthrough enables label-free detection and high-throughput analysis of hundreds of proteins in a few minutes.
Researchers create synthetic ring teeth proteins with varying repeats to achieve programmable materials with improved strength and flexibility. These self-healing polymers can be tailored for specific properties, such as elasticity and plasticity, making them suitable for various applications in textiles, cosmetics, and medicine.
A team of researchers from Université de Genève and EPFL found that the HOX13 architect proteins play a crucial role in the formation of both arms and hands. The study reveals how a genetic switch allows for a clear boundary between these two developmental processes.
Researchers discovered a crucial connection between protein structures and molecular functions by analyzing ancient genetic sequences. They found that tiny gene segments determine the formation of active sites in proteins, enabling them to perform specific functions.
Researchers at the Medical University of South Carolina discovered Myo1c's role in transporting Neph1, a protein essential for maintaining podocyte function and effective kidney filtration. Understanding this transport mechanism may lead to therapeutic targets for treating glomerular diseases.
Case Western Reserve University researchers have discovered the full-length structure of the TRPV2 protein, a potential target for pharmaceutical research in treating chronic pain and cancer. The study reveals TRPV2's molecular mechanism in neurite growth and its involvement in malignant cancer cells.
Researchers have determined the near-atomic level map of Zika virus, showing a notable difference in one key surface protein compared to other flaviviruses like dengue. This structure may provide clues for understanding how Zika enters human cells and suggest ways to combat the virus with drugs or vaccines.
Chemists at the University of Illinois have identified the complex chemical structure of alpha-synuclein, a protein that forms long fibrils in the brains of Parkinson's disease patients. This knowledge will help researchers identify specific targets for diagnosis and treatment.
A team of researchers at UMass Amherst and Virginia Tech have identified the factors governing the final morphology of self-assembling chiral filament bundles. Their new model predicts the size and shape of these structures based on molecular-scale interactions, providing insights into protein fiber formation in various tissues.
Baylor College of Medicine researchers have developed a new mathematical tool that combines biochemistry and computational analysis to identify specific structural changes in the dopamine 2 receptor, which helps maintain its structure and function throughout an evolutionary time scale. This discovery opens the possibility for better dr...
Researchers solved the structure of a key coronavirus protein, revealing its conformation and potential vulnerabilities. This finding could guide future treatments for viruses like SARS and MERS.
The University of Missouri has received a $1.3 million NIH grant to improve protein structure prediction using deep learning techniques. The research aims to increase the accuracy of predicting protein structures, which is crucial for breakthroughs in drug discovery, precision medicine, and disease detection.