The study used Fourier transform infrared spectroscopy to detect biomolecular changes in white blood cells stimulated with bacterial components, revealing a threefold increase in microvesicle production and altered lipid content.
New research by University of Bristol physicists shows that protein molecules can be understood using virtual knots, a branch of knot theory previously considered abstract. This approach captures the essential ambiguity of where protein curve ends are, providing a more detailed understanding of their three-dimensional structure.
Chemists have developed a new technique called redox activated chemical tagging (ReACT) that selectively links chemicals to proteins. This method could transform the way drugs are developed, proteins are probed, and molecules are tracked and imaged.
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Researchers at the University of Kentucky have discovered ten previously unknown microbial natural products from an abandoned coal mine in Kentucky. The compounds include four new geldanamycin variants and four McCrearamycins, which contain a cyclopentenone ring. These findings suggest that small structural variations can impact cell u...
Researchers have shown that weak attraction forces between proteins can greatly impact diffusion in densely concentrated protein molecules, similar to those found in living cells. This phenomenon has significant implications for understanding biological processes and their regulation.
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 supercomputing to simulate protein motion over a huge range of timescales, revealing self-similar dynamics and out-of-equilibrium phenomenon. This breakthrough has significant implications for advancing energy and medical sciences.
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Biochemists at Oregon State University have made a fundamental discovery about protein structure that sheds light on how proteins fold and change shape. The findings reveal the first direct views of specific details of one aspect of protein folding in a way that had not been considered possible.
Researchers have discovered an intricate dance of protein motion, where temperature sets the tempo, allowing for a deeper understanding of biological mechanisms and potential treatments. This new knowledge could lead to breakthroughs in disease cures and compound production.
A new study by University of Notre Dame researchers found that the most abundant protein in the Ebola virus, VP40, mediates replication and interacts with human cell lipids. This discovery may lead to novel therapeutics for combating Ebola.
Researchers created a 24-atom protein assembly that self-assembles into a porous molecular cube. This breakthrough could lead to the development of synthetic vaccines and targeted medicine delivery inside human cells. The discovery was made by UCLA biochemists led by Todd Yeates.
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Researchers design manmade proteins with new structures, including central cavities, to enhance biological functions and create novel molecules. The discovery is part of the growing field of synthetic biology at the University of Bristol.
Researchers at the University of Glasgow discovered that proteins like lysozyme can vibrate at frequencies similar to a few terahertz, allowing for efficient biochemical reactions. This 'ringing' motion enables proteins to morph quickly and bind with other molecules, critical for life's biological functions.
Researchers have developed a new method to refine low-resolution X-ray crystallography data for biomolecules, combining PHENIX and Rosetta software. The new approach can aggressively optimize models to fit the data while presenting realistic geometry.
Researchers have found that lactoferrin has various health benefits, including wound healing and protection from bacterial, viral, fungal and protozoal infections. The protein is also being explored as a potential therapeutic agent for cancer prevention and treatment.
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Scientists discovered a gene mutation causing hereditary spastic paraplegia, which may provide clues to axon degeneration in conditions like multiple sclerosis. The study highlights new disease mechanisms that could lead to genetic counselling and testing for affected families.
Dr. Oliver Daumke has won the Bayer Early Excellence in Science Award for his work on G proteins, which play a crucial role in cellular signaling pathways and immune response. His research holds promise for developing new strategies to treat diseases such as cancer, diabetes, and flu.
Researchers at Michigan State University found that protein diffusion is slower than previously thought, which could lead to new therapeutic strategies for diseases such as Alzheimer's, ALS, and cystic fibrosis. The discovery provides a fundamental understanding of the pre-folded state of proteins.
Researchers at TUM have successfully manipulated a single 'zipper' protein molecule to map changes in its energy landscape during folding and unfolding. This breakthrough provides higher-resolution measurements of protein folding dynamics, shedding light on the chain of events leading from DNA coding to biological function.
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Researchers at the University of Rochester Medical Center have designed a new version of factor VIII that doubles its ability to bind with factor IX, potentially reducing costs and immune reactions. The redesigned protein accelerates blood clotting, offering a promising alternative for next-generation hemophilia treatment.
Protein nanostructures have been created using a novel method that allows for precise control over their shape and size. The technique involves the use of nanoparticles to guide the assembly of protein molecules into specific structures.
Researchers have discovered a virus with an armored coat made of interlocking rings of protein, similar to medieval chain mail suits. The discovery could lead to new designs for nanotechnology, as the unique structure allows for stability while maintaining mobility.
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Chemist Peter G. Wolynes explains how glass, a disorganized crystal in a frozen state, keeps its shape and applies this insight to study protein structures. His work has numerous applications in environmental cleanup and drug design.
Chemist F. Ann Walker received the Francis P. Garvan-John M. Olin Medal for her research on heme proteins, including nitrophorin, a molecule found in kissing bugs that releases nitric oxide to facilitate feeding. Her work provides insight into the function of heme proteins and their role in the immune system.
A study found that metallothionein levels increase in the brain in response to alcohol consumption, suggesting a potential protective role. Higher MT levels may explain different levels of alcohol-related toxicity in individuals.
Researchers found that a short distance of 2.53 angstroms between iron atoms in peroxide-bridged ferritin intermediate favors biomineralization process over oxygen activation. The study uses analytical techniques to probe molecular structure and collaboration with experts from different disciplines.
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The U-M research will systematically study the proteins made by tumor cells, genes that instruct them, and subtle differences among proteins from different types of tumors. The goal is to develop rapid-analysis technology to detect cancer early and predict treatment response.
Researchers at Mayo Clinic Jacksonville developed a new type of molecule that can block neurotensin's ability to lower body temperature and reduce pain sensation. The breakthrough could lead to drugs specifically created to fight diseases at the molecular level.
Researchers found a protein called GON-1 that regulates organ shape in Caenorhabditis elegans, a microscopic worm. This discovery could lead to the development of inhibitors to slow or stop cancer cell spread and may one day enable growing human organs in labs.
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Researchers used new techniques to study HDL particles, verifying the lipid bilayer structure and confirming a key finding about protein orientation. The study resolves a long-standing controversy over the structure of HDL, shedding light on its role in cardiovascular health.
A new sulfoxide hydrogel polymer enhances water levels in the eye while minimizing protein buildup, leading to softer lenses that are more comfortable and breathable. Clinical trials have begun for these innovative contact lenses, which could become available as early as next year.
Protein folding research is undergoing explosive growth, revealing secrets of spontaneous self-assembly process, according to an editorial by Jay Winkler and Harry Gray. The study focuses on chemical kinetics and includes real-time observations, advancing efforts to design new drugs and decode genetic information.
Researchers successfully engineered a hybrid enzyme with improved substrate specificity, demonstrating the potential of recombining subdomains to generate novel functions. The study presents a method for generating hybrid genes by combining subdomain segments from diverse proteins.
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A protein called osteogenic protein-1 (OP-1) may speed the recovery of stroke patients by rewiring damaged brain cells. The experiment used rats and showed that OP-1 helped them recover lost movement in their limbs quickly, outperforming those in a control group.
Scientists have found that parts of the protein shell of the common cold virus flap open in a motion called "breathing", which can be stifled by compounds that stop viruses from infecting cells. This discovery could lead to rapid screening methods for antiviral drugs.
Researchers at the University of Notre Dame discovered that Factor VII deficient mice embryos developed normally throughout gestation, despite suffering fatal perinatal bleeding after birth. The study suggests a new avenue for exploration of coagulation proteins' role in embryonic development.
A new software developed by Ohio University researchers reduces amino acid sequence misidentification rates by at least twice, combining human intelligence with automated systems. The software aims to minimize time spent on identifying protein sequences, improving accuracy and efficiency in biochemistry research.