Articles tagged with Protein Structure
The Center for Structural Genomics of Infectious Diseases and the Seattle Structural Genomics Center have experimentally determined 500 three-dimensional protein structures from bacterial and protozoan pathogens. These structures could lead to the development of new drugs, vaccines, and diagnostics to combat deadly infectious diseases.
Researchers have determined the atomic-scale arrangement of proteins in a virus structure that enables it to invade and fuse with host cells. The findings show how the structure morphs in response to changing acidity, exposing a portion required for fusion with the cell membrane.
The structure of Lassa virus protein reveals how it evades the host's immune system and hijacks infected cells' machinery. Scientists discovered a unique mechanism called cap-stealing, where the virus steals the host cell's RNA cap to suppress interferon production.
Scientists have solved the structure of a protein integral to maintaining healthy hearts and nervous systems. The discovery of cystathionine beta-synthase (CBS) may lead to smarter drug design for better understanding of homocystinuria, a genetic disorder affecting cardiovascular and central nervous systems.
MoDEL, a new database of protein motions, was published by IRB Barcelona scientists. The database holds over 1,700 proteins and allows for more accurate drug design.
A team of researchers has created a technology to extract complex membrane proteins without distorting their shape, enabling scientists to better understand the properties and functions of these proteins. This breakthrough could facilitate research at the biomedical frontier.
Scientists have developed a bioinformatics strategy to predict membrane protein structures, which are underrepresented in existing databases. Using this approach, researchers successfully determined the tertiary structure of a bacterial membrane protein and predicted the structure of a plant membrane protein.
Rutgers University has received a $47.5 million grant from the NIH to study protein structures and their impact on diseases. The grant supports two major programs: NESG, which develops new methods for determining protein structures, and SBKB, which collects and disseminates protein structure information worldwide.
The Einstein research aims to understand the role of proteins in normal biological processes and disease pathways. The project will focus on determining the structures of thousands of biomedically important proteins.
The NIH has awarded $290 million in grants for structural biology research, focusing on determining protein shapes and functions. Four large-scale centers will operate pipelines for protein structure determination, including centers for mitochondria and membrane proteins.
The NIH has awarded a $7.7 million grant to Arizona State University to unravel the structures of membrane proteins that play a key role in protecting against infectious diseases. The ASU center will target membrane proteins of key viral and bacterial pathogens, their infectious pathways and molecules involved in host defense.
The National Institutes of Health has awarded $11.5 million to a consortium of research institutions led by the California Institute of Technology for a center focused on studying membrane-protein structures, aiming to shed new light on basic biology and potential treatments for disease.
Researchers at Helmholtz Zentrum Muenchen and TU Muenchen used NMR spectroscopy to determine the spatial structure of Sam68's Qua1 region, essential for dimerization and biological function. The study sheds light on Sam68's role in cell cycle regulation and cancer pathogenesis.
Brown University researchers have discovered the structure of three types of proteins that don't have a fixed shape, revealing how they interact with other proteins to regulate important biological processes. The findings provide new insights into the complex mechanisms underlying these proteins' functions.
A new study reveals that Foldit players have successfully solved protein-folding problems that are too difficult for supercomputers, using intuitive leaps and strategic thinking. The game has shown promise in tackling medical challenges, such as designing proteins to combat diseases like the flu and HIV.
The Foldit game harnesses distributed thinking to predict protein structures, outperforming computers in some cases. Non-scientists excel at the game due to its reliance on visualization skills, and humans have proven better than computers in certain tasks.
Scientists at Tufts University and the University of Pennsylvania have determined the unusual structure of a key member of the herpes virus protein complex that allows it to invade cells. The research provides a new target for antiviral drugs, which could prevent the virus's access to cells.
Researchers at VIB's Jean Jeener Bio-NMR Center discovered how bacterial proteins regulate stress response via dynamic allostery, a previously theoretical concept. This breakthrough uses NMR technology to visualize protein folding and conformational changes.
Researchers at NPL have confirmed a definitive structure of an HIV protein, shedding light on its infection mechanism. This discovery may lead to better treatments for people affected by HIV.
The National Institute of General Medical Sciences has granted $1.18 million to the University of Missouri to improve their protein prediction software, MULTICOM. The system can help scientists design drugs by predicting protein structures in diseases.
Scientists from Freiburg and Berlin have unraveled the secret of the Mx protein, which plays a crucial role in inhibiting influenza virus replication. The Mx protein forms a ring-structured macromolecular network that restrains and deactivates viral components, providing a defense mechanism against new flu viruses.
Scientists propose general rules governing the assembly of filaments into thicker and twisted ribbon-like fibers using Atomic Force Microscopy images and polymer physics concepts. The model accurately predicts the formation of Amyloid fibers, with potential applications in understanding neurodegenerative diseases.
Scientists have uncovered key rules governing ferritin's self-assembling nanostructure, enabling potential breakthroughs in drug development and nanotechnology. The study may lead to creating biological nanostructures with precise dimensions for various applications.
Researchers created super-strong collagen with improved stability, which could treat conditions like arthritis by mimicking natural collagen. The new collagen holds together at high temperatures and has a similar three-dimensional structure to natural collagen.
Researchers at the University of Illinois have designed a synthetic protein that mimics both the structure and function of nitric-oxide reductase, a key enzyme in the nitrogen cycle. The protein, which uses myoglobin as a scaffold, provides an excellent model for studying this enzyme and creating biocatalysts.
Scientists at Boston Biomedical Research Institute discovered that combining EGCG and DAPH-12 can prevent and destroy various protein structures known as amyloids, which are primary culprits in fatal brain disorders. The study may contribute to future therapies for Alzheimer's, Huntington's, and Parkinson's diseases.
Researchers at the University of Gothenburg have developed a new technique that allows for precise analysis of protein sugar structures. This breakthrough may lead to a better understanding of disease mechanisms and potential new treatments, particularly for conditions such as Alzheimer's.
Researchers at Lund University have discovered that proteins change structure and stick together to form structures believed to underlie ALS. The discovery opens the possibility of designing drugs to prevent misfolding and its fatal consequences.
Researchers at the Monell Chemical Senses Center discovered that oleocanthal alters the structure of neurotoxic beta-amyloid proteins, impairing their ability to damage brain nerve cells. This structural change makes oleocanthal a potential target for developing effective immunotherapy treatments.
The Biophysical Society has recognized ten new fellows for their exceptional contributions to the field of biophysics. These researchers have made significant advances in understanding the structure and function of biological macromolecules, membrane proteins, and biomembranes through innovative approaches and pioneering techniques.
The Case Center for Synchrotron Biosciences will provide three Technology Cores to support the study of proteins and nucleic acids. The center's facilities will enable researchers to understand the structure and function of proteins, including in vivo studies, as well as investigate the role of metal atoms in proteins.
Researchers at the University of Pittsburgh School of Medicine have found that proteins have an intrinsic ability to change shape, allowing them to select the structure that permits the best binding. This discovery could lead to more effective treatment of diseases by designing compounds that target specific protein structures.
Scientists at UGA develop model showing loss of key protein can lead to aneuploidy, a condition causing birth defects. The research also opens possibility of engineering 'artificial chromosomes' into corn varieties for improved traits.
A team of scientists at TUM has successfully determined the three-dimensional structure of αB-crystallin, a key protein that protects against cataracts. The discovery sheds new light on the molecular architecture of this protective protein and may lead to the development of new treatments.
A team of scientists used fluorescence technique to find a bacterial protein can shift between two stable structures, one active and the other inactive. The discovery sheds light on how proteins regulate cellular activities through shape-shifting.
Researchers have gained insight into the regulation of aquaporins in yeast cells, revealing a previously mysterious region that acts as a gate controlling water flow. This discovery may lead to the development of inhibitors for human aquaporins, which could slow down cancer tumor growth.
Researchers have determined the molecular structure of a plant photolyase protein similar to two cryptochrome proteins controlling the human clock. The study reveals key differences between human and plant cryptochromes, shedding light on the complexities of the human sleep/wake cycle.
A new study of protein structures reveals a 'big bang' of innovation, coinciding with the emergence of three superkingdoms. The study constructs a timeline of protein evolution that relates directly to the history of life.
Researchers at the University of Leeds have discovered that proteins fold incorrectly many times before forming the correct structure, with amino acids central to function causing misfolding. The study, which looked at the Im7 protein, has huge implications for understanding protein sequences and disease balance.
Researchers at Rensselaer Polytechnic Institute have developed a targeted strategy to substantially increase the thermodynamic stability of nearly any protein while preserving its unique function. The design technique creates proteins that remain stable at temperatures 10 degrees Celsius higher than normal.
The study solved the structure of a biological protein from the vaccinia virus, providing insights into its relationships with other viruses. This discovery is significant as it can help develop new therapies to treat various viruses, offering potential solutions to outbreaks and pandemics.
MIT researchers discovered a simple arrangement of proteins produces sturdiest product with great strength and robustness. The optimal composition includes two repeated hierarchies of alpha-helical proteins, providing the basis for optimal material performance.
Researchers have solved the structure of VP35, a key part of the Ebola protein that interferes with host cell defense mechanisms. This discovery paves the way for designing drugs that can bind to and inhibit VP35 function, potentially neutralizing the Ebola virus.
Researchers have redesigned factor VIII to increase its ability to drive blood clotting, which could lead to more effective and less burdensome hemophilia treatment. The new design improves the stability of the protein, allowing it to withstand manufacturing processes and exposure to the human bloodstream.
David Baker, a UW professor, won the 2008 Raymond & Beverly Sackler International Prize in Biophysics for developing accurate computer models of protein structures using Argonne's Leadership Computing Facility. His work has led to new insights into protein functions and potential therapeutics.
Scientists have obtained the first 3D images of the Mcm10 protein, which is essential for DNA replication in eukaryotic cells. The structure reveals unique features that allow it to interact with single-stranded DNA and position other proteins on the DNA strand.
Scientists have discovered that a protein banished from mature axons allows them to transform into dendrites. This process could occur after nerve cell damage, raising possibilities for the reverse transformation.
The study provides a detailed understanding of the human A2A adenosine receptor, shedding light on its structure and potential drug targets. The findings suggest that the receptor has varying binding pockets, yielding opportunities for receptor diversity and ligand selectivity.
Researchers at UVA Health System develop novel approach to create less resistant and more effective antibiotics by targeting integral membrane enzyme DsbB. The breakthrough uses nuclear magnetic resonance spectroscopy to understand protein structure and function.
The Biophysical Society has awarded eight individuals in recognition of their groundbreaking work in biophysics. Robert Stroud and Stephen H. White were recognized for their pioneering research in transmembrane biology and lipid structure, respectively.
Researchers have determined the 3D structure of UHRF1's Set and Ring Associated domain, crucial for ensuring accurate epigenetic code copying. This breakthrough facilitates a better understanding of epigenetics and its role in cancer development.
Researchers at NYU and AMNH will model two plant species, Arabidopsis thaliana and Oryza sativa, using bioinformatics to gain insights into protein structure and function. The project aims to annotate the functions of unknown proteins in plant genomes, shedding light on their roles in cellular processes.
Iowa State University researcher Robert Jernigan's study reveals proteins have controlled motions, contradicting traditional biochemist views. The research, published in journal Structure, shows that protein motions are restricted and part of the function of the proteins.
Researchers describe a new computer-based technique to identify tau protein structures associated with Alzheimer's disease, offering hope for new treatments. By analyzing experimental data, they found one structure likely to play a role in the pathologic process.
Researchers at the University of Illinois have developed a new technique to determine the atomic-scale structure of membrane proteins using solid-state nuclear magnetic resonance spectroscopy. This breakthrough enables high-resolution structural information, which is crucial for understanding protein function.
The American Society for Biochemistry and Molecular Biology (ASBMB) has selected eight scientists for its annual awards competition, recognizing their contributions to science. The award winners include David Davies, John Kuriyan, Sarah Spiegel, Susan Lindquist, Douglas Rees, Phillip Zamore, Sandra Schmid, and Rochelle Schwartz-Bloom.
Researchers describe the shape of the Ebola virus spike protein bound to an immune system antibody, providing a major step forward in understanding how the deadly virus works. The structure reveals vulnerable sites that can be exploited to develop potential Ebola virus vaccines or treatments.
Cure Lab, Inc. has developed a new technology that combines two forms of vaccine antigens: one easily processed by the proteosome and another resistant to it. This combination elicits a stronger immune response than using either form alone, promising improved vaccine efficiency.
Scientists have identified a crucial portion of a protein responsible for hereditary cerebral amyloid angiopathy (CAA), a disease linked to stroke and dementia. The study used solid-state nuclear magnetic resonance (NMR) spectroscopy to reveal the structure of CAA fibrils, which form plaques in blood vessels in the brain.
Researchers at Medical College of Wisconsin discover that lymphotactin, a key immune response protein, rapidly shifts between two unrelated structures up to ten times a second. This finding may lead to new insights into misfolded proteins like Alzheimer's and Parkinson's diseases.