Articles tagged with Protein Structure
Researchers have uncovered the structure of a protein complex responsible for adding sugar molecules to proteins, crucial for many protein functions. The discovery may help understand diseases resulting from faulty glycosylation processes.
University of Minnesota researchers have determined the atomic structure of APOBEC3G, a protein that inhibits HIV-1 infection. This discovery will help researchers manipulate the protein to combat HIV and develop methods to neutralize Vif, which triggers the destruction of APOBEC3G.
Researchers at UCLA have modeled the structure of large cellular particles, known as vaults, which may function in innate immunity. The study proposes ways to engineer these particles for targeted release of drugs.
A new study from Rice University and the University of Houston found that proteins pack more tightly in their natural environment, with increased structural content and stability. The research suggests that protein structure is affected by crowding, even when proteins are in their folded state.
A team of researchers has explained the discrepancy between computer simulations and experimental observations of protein behavior under mechanical stress. At slower speeds, hydrogen bonds in proteins behave differently, breaking three at a time when pressure is applied slowly.
Researchers at HHMI used a new computational method to predict protein structure with remarkable accuracy. The method, called Rosetta@home, uses distributed computing and targeted rebuilding to overcome challenges in predicting protein structures.
Researchers compiled global census of protein architectures to plot evolution of Archaea, Bacteria, and Eukarya. The study found evidence that archaeal microbes emerged first as an evolutionarily distinguishable group, losing a fold in the process.
A multidisciplinary team led by UCSD researchers has determined the structure of MitoNEET, a protein that shows promise as a target for developing innovative diabetes drugs. The discovery provides insights into how these drugs may protect cells from oxidative stress and potentially offer greater specificity and fewer side effects.
A recent study published in Nature Genetics has found a genetic mutation linked to systemic lupus erythematosus, a complex autoimmune disease. The discovery identifies variations of the TREX1 gene as a risk factor for developing lupus, shedding new light on its causes and potentially paving the way for new treatments.
Researchers at Hauptman-Woodward Institute have solved the structure of a novel protein in Pseudomonas, a bacterium that causes cystic fibrosis and tuberculosis. The discovery may lead to the development of new antibiotics to prevent infection in patients with CF and TB.
A research team led by UCSD scientists has discovered how genetic mutations affect the structure of proteins implicated in autism spectrum disorders, contributing to developmental abnormalities. This study represents a solid starting point for understanding the disorder and developing new drug therapies.
The study suggests that structural modules in yeast protein-protein interaction networks originated as evolutionary byproducts without functional units. Computer simulations show that modular structures can arise during network growth through simple models of gene duplication.
Researchers created a global family tree of metabolic protein architecture using phylogenetic analysis techniques. The study found that many metabolic protein folds are quite ancient, with some common in all species analyzed, while others are more recent.
Scientists at the Universidad Nacional Autonoma de Mexico and Buck Institute created an algorithm that identifies critical protein elements solely based on their shape. This breakthrough enables more efficient development of effective treatments and diagnostic tests for various diseases.
The Structural Genomics Consortium has determined the 3D structure of PARP3, a protein of significant relevance to diseases such as cancer, inflammation, and metabolic disorders. The available data can accelerate early-phase drug development projects and contribute to a better understanding of disease mechanisms.
Researchers predicted 3D structures for yeast proteins using de novo methods and integrated with biological data, providing a global view of protein relationships. The study assigned domains to families of evolutionarily related proteins, generating testable hypotheses about their mechanisms of action.
A new theory by FSU researchers accurately predicts the association rate for proteins, a critical factor in biological processes. The theory could lead to more effective treatments for genetic disorders and other life-threatening conditions.
Researchers at Columbia University Medical Center have uncovered the complex structure of AMP-activated protein kinase (AMPK), a central energy gauge for cells. This discovery provides crucial details about the molecule necessary for developing new therapies for diabetes and obesity.
Researchers at Yale University have created a protein-like molecule using beta-amino acids, which could have been the natural building blocks of life. The discovery shows that peptides assembled from these non-natural building blocks can fold into structures similar to natural proteins.
Researchers describe a unified description of electron movements through certain proteins, uncovering key pathways that optimize energy harvesting in photosynthesis and animal cells. The study reveals complex routing options that allow electrons to take shortcuts, increasing the challenge for theoreticians.
A team of researchers at the University of Pennsylvania School of Medicine has identified a molecular spring within the fibrinogen protein, which explains how blood clots can stretch and bend under physical stress. This discovery may lead to the development of treatments for cardiovascular diseases such as stroke and thrombosis.
Scientists from IRB Barcelona have published a dynamic map of protein behavior, enabling the prediction of protein structures and interactions. The study, part of the MoDel project, aims to establish a 'fourth dimension' for protein structures, facilitating the design of new drugs and understanding of protein functions.
Researchers at Brown University have solved the structure of a DNA-protein complex that aids in site-specific recombination, a process that allows mobile DNA to cut into chromosomes. The discovery provides new insights into how this process shapes species over time and its role in spreading antibiotic resistance and certain diseases.
Researchers discovered that present-day organisms use trace metals derived from ancient changes in ocean chemistry. Protein structures revealed a major influence of geochemistry on life, leading to diversification and complexity. The study links biology and geology, shedding light on co-evolutionary processes.
The MIT team analyzed 32,853 proteins and found the most complicated knot, a five-crossing trefoil knot, in only one protein. This knot may prevent the protein from getting sucked into the proteasome as it works, supporting the theory that complex knots are linked to the protein's function.
Researchers at the University of Illinois developed MultiSeq, a free software that analyzes sequence and structure data to investigate changes in proteins and nucleic acids. This allows scientists to gain insight into fundamental questions like the origin of life and develop resistance to antibiotics.
Researchers at IRB Barcelona have identified a crucial protein in building the nuclear envelope, a complex structure surrounding the nucleus. The discovery of MEL-28 sheds light on how this envelope is assembled and regulated.
Researchers at NC State University have characterized the shape of calbindin-D28K, a protein linked to neurodegenerative diseases. The protein's flexibility and ability to bind to caspase-3 may provide insights into developing drugs to halt disease progression.
A team of researchers has designed tools to accelerate interpretation and potential use of human genome project information. The Joint Center for Molecular Modeling will support scientists in developing innovative software for improving protein structure prediction quality.
The Human Proteome Folding project aims to predict the structures of human proteins using idle computer cycles from millions of users. The NYU researchers will focus on cancer biomarkers and host-parasite interactions, refining predictions with more accurate methods.
The Salk Institute researchers created a cell-free system to study the insertion of nuclear pore complexes into the nuclear membrane. Using advanced imaging tools, they observed the formation of nuclear membranes and pores within an hour.
A new study describes the structure of an H5 protein from a highly pathogenic strain of H5N1 avian influenza virus, comparing it to other pandemic influenza A viruses. The research also discusses a potential route for H5N1 to mutate and acquire human specificity.
The Compact Light Source (CLS) is a mini-synchrotron that can produce intense X-ray beams in the space of a small office. The CLS will be installed at the Scripps Research Institute to accelerate protein structure determination, potentially advancing biomedical research.
GlycoFi researchers have made a major leap in protein bioengineering by controlling sugar structures on antibodies to boost cancer-killing ability. This approach can be applied to any therapeutic glycoprotein, and the company is poised to capitalize on the growing 20% annual growth of the therapeutic protein market.
Researchers have obtained the crystal structure of phytochrome, a protein that regulates plant growth and development in response to light. The discovery may lead to precise control over flowering events and improved crop yields.
Yale researchers have developed a method to count absolute numbers of individual protein molecules inside living cells and measure their locations with high accuracy. This breakthrough addresses fundamental hurdles for studying biology quantitatively, enabling the measurement of protein concentrations in various cellular structures.
Small single-domain proteins, often referred to as 'two-state folders', fold into their three-dimensional structures by crossing only a single barrier. A new interpretation of mutational data suggests that this process involves a fully formed helix in the transition state.
Researchers found that abnormally long glutamine tracts in proteins can cause nerve cells to deteriorate and die. The study suggests that understanding the molecular mechanism behind polyglutamine diseases may lead to the development of new treatments, including small molecule drugs.
Scientists at UT Southwestern Medical Center have developed a method to create artificial proteins based on evolutionary patterns, sharing similarities with natural proteins. The new approach allows for the reconstruction of modern-day proteins with high accuracy.
Scientists have made significant progress in predicting protein structures using computers. The Rosetta program uses a two-step process to generate energy calculations and select the lowest energy shape as prediction. This approach has achieved almost atomic resolution in structure prediction for about one-third of small proteins.
Rensselaer researchers have developed a predictive modeling approach that can determine protein behavior for use in bioseparation applications. The model uses molecular information obtained from the protein structure to predict adsorption isotherm parameters and chromatographic behavior, replicating experimental results.
Researchers at Brown University have solved a crucial part of the SAP97 protein's structure, allowing them to develop a molecule that can inhibit it. This breakthrough could lead to effective treatments for cardiac and neurological diseases, including learning and memory disorders and drug addiction.
The Protein Structure Initiative will accelerate structure determination of thousands of proteins, enabling predictions of protein functions and discovery of new drug targets. Rutgers' NESG is a key member of the PSI network, leveraging its expertise in structural biology to advance biomedical research.
The Protein Structure Initiative aims to determine protein structures to reveal their roles in health and disease. Columbia researchers will contribute to three centers, focusing on membrane proteins and cancer-related proteins.
The Protein Structure Initiative (PSI) has reached its rapid production phase, aiming to determine thousands of protein structures using innovative approaches and tools. The new centers will use methods developed during the pilot period to rapidly generate protein structures found in organisms ranging from bacteria to humans.
The Joint Center for Structural Genomics will determine a large number of high-resolution structures of biological molecules using new methods and technologies. The researchers aim to tackle challenging structures such as large protein assemblies and proteins essential for all organisms.
A Massey Cancer Center researcher has identified the atomic structure of angiopoietin-2, a key protein involved in the neo-vascularization of solid tumors. This discovery may lead to better exploration of how to turn off cancer growth signals and identify potential therapeutics.
Researchers at the Weizmann Institute of Science have determined the structure of a protein complex on retroviruses that enables them to infect cells. The complex undergoes a radical change in shape as it attaches to cells, and its arrangement is unlike other known viral envelope protein structures.
Researchers at Rice University discovered that eight conserved amino acids in sandwich-like proteins are essential for stabilizing the final structure, while also directing the process of protein folding. This finding provides new insight into the interplay between protein evolution, structure, and folding.
A study published in Nature Structural & Molecular Biology has uncovered the structure of resuscitation promoting factor (Rpf), a key player in TB bacteria. The discovery holds promise for developing new methods to 'wake-up' dormant bacteria, allowing antibiotics to kill and cure the disease.
A team of researchers from Howard Hughes Medical Institute and the University of Washington designed a novel protein with atomic-level accuracy using computer-aided design. The breakthrough allows for the exploration of previously unseen regions of the protein universe, opening up new possibilities for studying protein-folding energetics.
Researchers at Temple University have discovered a new family of genes that could serve as a potential cancer marker. One form of the gene, NSP5a3a, is highly expressed in some tumor cell lines and may be useful for developing diagnostic tests and cancer therapies.
Researchers have discovered a new protein, SP-1, with unique structural characteristics that can survive extreme conditions. The protein has the ability to assemble into a structure composed of 12 identical units, making it exceptionally resistant to conditions and promising for medicinal applications.
The study reveals how botulism-causing Clostridium botulinum detects nitric oxide, shedding light on its role in human cardiovascular, neurological, and immunological systems. The research also provides insights into the structural details of soluble guanylyl cyclase, a protein difficult to crystallize for analysis.
Researchers have developed a mathematical algorithm called TANGO that can predict the likelihood of proteins sticking together incorrectly. This could lead to new diagnostic techniques for diseases caused by misfolded proteins, such as Alzheimer's and Parkinson's, and more efficient production of therapeutic proteins.
Matthew Bottomley, a researcher at the European Molecular Biology Laboratory, has won the 2004 EMBO Science Writing Prize for his captivating article on bioluminescent squid. The prize of 1,500 Euro will be presented to him at the EMBO Members Meeting in October this year.
Researchers characterized intermediate states in protein folding at an atomic level, a crucial step towards predicting protein structure and improving drug design. This breakthrough could help understand errors in folding linked to diseases like cystic fibrosis and Alzheimer's.
Researchers used a new mass spectrometry technique to determine how CENP-A turns a chromosome's center section into a stable centromere. The study sheds light on the process of cell division and its connection to birth defects and cancer.
Researchers have developed new algorithms to interpret NMR data, revealing protein structure and molecular architecture. The tools require less data while producing highly accurate results.
A team of researchers has developed a new technique to directly measure protein binding forces, clarifying the role of membrane-anchored protein NCAM in cell adhesion. Their study reveals that NCAM forms two adhesive configurations, which are validated by experimental results and contribute to spatially distinct bonds.