Articles tagged with Structural Biology
Researchers at the University of Leeds captured images of motor protein dynein in action using electron microscopes. The study revealed a hinge between the motor's arms and its track, allowing flexibility in movement.
A new study has provided never-before-seen details of the human body's cellular switchboard that regulates sensory and hormonal responses. The research, led by Eric Xu at the Van Andel Research Institute, used SLAC's X-ray laser to complete the first 3-D atomic-scale map of a key signaling protein called arrestin.
Researchers developed an RNA dynamics model using beads and springs, achieving accurate predictions comparable to Molecular Dynamics simulations. The model's simplicity allows for near real-time processing and may be a viable alternative to expensive computer simulation methods.
Researchers have discovered that spider and centipede venom originated from an insulin-like hormone, with similar molecular shapes between the toxins and the hormone. This finding has potential applications in developing new pharmaceuticals and bioinsecticides, as well as solving agricultural and medical problems.
Researchers have determined the basic structural organization of the dynein-dynactin complex, a molecular motor responsible for cellular activities such as cell division and intracellular transport. The findings shed light on diseases like Alzheimer's, Parkinson's, and ALS, and could lead to new treatments.
Researchers found no knots in RNA structures among 6,000 known chains. Instead, naturally occurring RNAs tend to form simple geometric configurations.
Researchers at Arizona State University have discovered a novel mechanism driving the evolution of green-to-red photoconvertible phenotype in green fluorescent proteins. The study reveals that hinge migration, driven by long-range dynamic motions, can lead to the acquisition of red fluorescence.
Researchers at Scripps Research Institute reveal new insights into nicotinamide nucleotide transhydrogenase (TH), a metabolic enzyme found in most forms of life, shedding light on its structure and function. The discovery sheds light on TH's dynamic structure and how it alternates functions to maintain cell health.
Scientists have developed a method to observe DNA double strand breaks, a process that lasts microseconds. They also created slow-motion films of the reaction by altering temperature and pH balance.
Six faculty members at Albert Einstein College of Medicine have been named 2014 AAAS Fellows, recognized for their contributions to various fields including virology, cell biology, and cancer research. The awardees include Aviv Bergman, Margaret Kielian, Richard Kitsis, U. Thomas Meier, Robert Singer, and Jan Vijg.
Scientists have unraveled a molecular mechanism of mRNA recognition, essential for understanding differential gene regulation in male and female organisms. This principle represents an essential and widespread mechanism of gene regulation in higher organisms.
A study at Oak Ridge National Laboratory reveals structural differences between normal and diseased forms of the huntingtin protein, which is involved in Huntington's disease. The researchers used neutron scattering to compare the structures over time, finding key discrepancies that support a growing focus on amyloid disorders.
A team of scientists has revealed the molecular mechanisms underlying Roquin's role in preventing autoimmune diseases. The study found that Roquin recognizes a range of RNA binding partners to control T-cell functions, regulating a larger number of genes than previously thought.
Research clarifies how bacterial red light photosensors change structure when sensing light, revealing amplification mechanism for rapid signal transmission. The study also sheds light on the molecular-level operating mechanisms of phytochrome proteins in plants.
The Price Family Foundation has awarded a $3 million grant to Albert Einstein College of Medicine and the University of Oklahoma to investigate the structural biology of anaerobic microorganisms, with a focus on combating C. difficile infections. The joint project aims to find better treatments for these life-threatening infections.
The University of Oklahoma and Albert Einstein College of Medicine will establish an Institute of Structural Biology to advance research on the impact of proteins. Researchers will target deadly diseases and search for new cures, gaining expertise in X-ray analysis and large-scale structural genomics.
Researchers at the University of York have discovered how one group of gut bacteria, Bacteroidetes, digest complex sugars found in fruits and vegetables. This understanding sheds light on nutritional issues like prebiotics and probiotics.
Researchers at Scripps Research Institute have developed a new method to map the 3D structure of membrane proteins, including the human serotonin receptor. This approach enables faster and more accurate imaging, potentially condensing the timeline for structural studies from months to days.
Researchers used X-ray laser to map the 3D structure of a key cellular gatekeeper, the human serotonin receptor. The breakthrough technique uses smaller crystals and produces high-resolution images, potentially condensing years-long studies into days.
Researchers have discovered that trees across species exhibit remarkably similar branching patterns, allowing scientists to infer a tree's function regardless of its shape or size. The study confirms a theory developed by UA ecology professor Brian Enquist and has implications for models used to assess forest ecosystems.
Researchers from UConn have captured the structural dynamics of a protein channel in the mitochondrion using fluorescent probes. The study reveals that the channel complex changes its structure in response to changes in the inner membrane's electrical field, providing new insights into how cellular transport systems harness energy.
Researchers identify unique properties of K11-linked polyubiquitin chains, suggesting new cellular processes involved in disease maintenance. These findings may lead to novel treatments for diseases like cancer and diabetes.
A team led by Peijun Zhang has described the 4-million-atom structure of HIV's capsid protein shell, revealing critical molecular interactions that could lead to new treatments. The findings may enable the development of drugs that disrupt the shell's assembly or disassembly, potentially stopping the virus from replicating.
Researchers at Helmholtz Centre and Technische Universität Darmstadt discover protein C4BP with eight 'arms' similar to a spider's web. This structure allows for potential use as a scaffold for drug transport, targeting pathogens more effectively.
Researchers propose a new theory of evolutionary development, suggesting that complex structures may emerge through the process of 'complexity by subtraction', where parts are lost or simplified over time. Computer models and trends in skull evolution support this idea, which challenges traditional incremental evolution.
Researchers at Virginia Tech Carilion Research Institute invent a way to directly image biological structures at their most fundamental level, providing a gateway to understanding dynamic systems in structural biology. The technique has successfully imaged viruses and other biological structures in their natural environments.
Researchers will use x-ray crystallography and NMR to understand the structural rules governing nuclear receptors' activity. The goal is to fill gaps in knowledge about these proteins' role in metabolism, cancer, inflammation, and bone health.
A University of Oklahoma research team has been awarded a $9.7 million NIH grant to study human diseases associated with aging, osteoporosis and diabetes. The grant will provide significant resources for investigators to pursue structure-based biomedical studies.
The university has upgraded its research facilities with a $2.7 million NMR spectrometer, allowing for faster and more detailed molecular imaging. This will enable researchers to study macromolecules at the molecular level, benefiting disease research and biological problem-solving.
University of Montreal researchers developed a strategy to monitor protein assembly by integrating fluorescent probes throughout the linear protein chain. This approach enables capturing snapshots of protein shape at each stage of assembly, shedding light on how proteins self-assemble into working nanomachines.
A study has identified an antitumor molecule originating from a cancer-causing gene that inhibits pro-cancer action of the oncogene. The finding could lead to discovering other oncogenes and anti-oncogenes, contributing to tumor development.
Researchers studied thale cress under high temperature conditions, finding that plants with reduced stomata exhibit greater water loss and leaf evaporative cooling. This adaptation may promote the diffusion of water vapor from stomata, cooling the plant.
Researchers are exploring X-ray imaging as a next-generation tool for gathering detailed structural and functional information on biomolecules. The technology has the potential to surpass traditional X-ray crystallography, enabling the study of complex biological systems in unprecedented detail.
Researchers at RIT and Dowling College are working on a three-year study to match the protein to its job in the human body. They will use a library of 400 protein motifs associated with known functions and compare proteins from the Research Collaboratory for Structural Biology Protein Data Bank with existing active-site templates.
Researchers at USC have found that the energy difference between two alpha-synuclein structures is less than previously thought, offering new insights into the protein's role in Parkinson's disease. This discovery could help explain why the protein misfolds and becomes toxic to surrounding nerve cells.
The 2011 Pew Scholars will advance research leading to medical breakthroughs and treatments, covering human diseases like Alzheimer's and diabetes. The program, investing over $125 million, recognizes early-career scientists with innovative ideas.
Researchers have identified a new target for combating cystitis: the thread-like structures on E. coli bacteria that adhere to bladder cells. Understanding this mechanism can lead to the development of new antibiotics, offering hope for treating recurring urinary tract infections.
Axel T. Brunger, a Stanford University professor, has been awarded the inaugural DeLano Award for Computational Biosciences for his work on structural biology and crystallographic refinement methods. The award recognizes his contributions to making computer technology accessible to the scientific community.
Researchers found that Hsp90, a common 'chaperone' protein, helps loose p53, contradicting its previous role in folding other proteins. This discovery adds to the growing knowledge of proteins' adaptability and activity in unfolded states.
The study completes the film frame of transporters' conformations, enabling understanding of diseases like cistinuria and design of drugs targeting cancer cells. New knowledge will help design inhibitors to affect amino acid uptake by cancer cells.
Scientists have successfully imaged an intact virus using extremely intensive and ultra-short x-ray pulses from the world's first X-ray free electron laser. This breakthrough technology enhances the possibilities of imaging individual biological molecules too small to study with conventional microscopes.
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.
The Joint Center for Structural Genomics (JCSG), led by Ian A. Wilson, has made significant strides in high-throughput structural genomics, solving over 1,150 structures to date. The JCSG's pipeline has optimized every stage of the process, enabling large numbers of target proteins to be tackled simultaneously.
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.
Researchers at Medical College of Wisconsin and University of California, Riverside create synthetic chemical mimicking abscisic acid to improve crop resistance to drought. The discovery paves the way for developing new molecules that activate or turn on receptors.
The Membrane Protein Structural Dynamics Consortium aims to unite structure and function through dynamic studies of membrane proteins, enabling better drug development for diseases like heart disease and diabetes.
The American Society for Biochemistry and Molecular Biology honored 11 researchers with various awards for their groundbreaking contributions to the life sciences. Axel T. Brunger, Michael Brown, Joseph Goldstein, Charles E. Chalfant, Job Dekker, Christine Guthrie, Arthur Gutierrez-Hartmann, Yusuf Hannun, and Arthur E. Johnson received...
Researchers have captured the 3D atomic models of a single transporter protein in its three main structural states, revealing the 'alternating access' mechanism. This discovery offers a detailed understanding of the function of essential chemicals entering cells and creates opportunities for developing new drugs.
A new study reveals that individual fibrin fibers play a crucial role in equitably distributing strain load and strengthening the entire network. The research found that fibers subjected to significant strain stiffen to resist stretch, thereby reducing strain concentrations.
Scientists have successfully imaged vesicles and filaments involved in neuronal communication, revealing crucial role of filamentous structures in regulating neurotransmitter release. The 3D images were obtained using electron cryotomography, a novel method that rapidly freezes cells while preserving biological structures.
A Notre Dame study highlights the role of dynamic motion by proteins involved in the body's immune response. The research found that different antigens produce distinct motions, complicating but also simplifying recognition by T-cell receptors.
Researchers at the University of Pittsburgh School of Medicine have identified a functional importance seam in the HIV coat that could lead to new treatments for blocking HIV infection. The findings may allow scientists to rationally design therapeutic compounds that interfere with assembly and function of the protein.
Researchers determine the three-dimensional structure of Pur-alpha protein, essential for normal neural function, and gain insights into its molecular function. The findings provide a possible basis for developing an effective therapy for Fragile X tremor/ataxia syndrome.
The National Science Foundation has awarded a $360,000 grant to establish a Robotics Crystallization Core Facility on the University of Oklahoma's Norman campus. The grant will provide sophisticated robotics equipment to support collaborative efforts among structural biologists in the state.
A team of researchers developed a technique to replicate biological structures on a nano scale, creating free-standing replicas of fragile, laminar, chitinous biotemplates. The resulting biomaterial could be used for optically active structures, such as optical diffusers for solar panels and devices with light-emitting properties.
The human genome is organized into two separate compartments, with active genes separated from inactive DNA. The fractal globule architecture enables cells to pack DNA densely while avoiding knots, allowing for efficient gene expression and replication.
Researchers discovered that an atomic force microscope's behavior changes when used in water, enabling the study of biological molecules' mechanical properties. The findings reveal details about a bacterial membrane and a virus called Phi29, shedding light on their intrinsic variations in local stiffness.
Researchers have gained in-depth knowledge of pyruvate carboxylase's structure, a metabolic enzyme linked to genetic diseases like lactic acidaemia and hypoglycaemia. The study also sheds light on its potential role in obesity and diabetes treatments.
Researchers at the University of Pittsburgh School of Medicine discovered a molecular '2-step' process that may lead to protein clumping in Huntington's disease. The study found that a slight lengthening of the polyglutamine sequence disrupts neighboring regions, initiating aggregation behavior. This discovery could provide new targets...
Researchers used Nuclear Magnetic Resonance Spectroscopy to study the tau protein's structure and interactions in neurons of Alzheimer's disease patients. The study found that abnormal phosphorylation of tau proteins disrupts their ability to bind to microtubules, leading to cell death and nerve damage.