Articles tagged with Protein Structure
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A study by UC Santa Barbara researchers found that a disordered protein exhibits slow relaxations, defying expectations, and 'remembers' its previous stretching. This behavior is similar to glassy materials like memory foam and crumpled paper.
Researchers have discovered a series of misfolded alpha-synuclein protein structures that are thought to be highly relevant to the onset of Parkinson's disease. These unique structures were found in the presence of phospholipids, which play an essential role in living cells, and take on a striking variety of shapes.
Researchers at UC Berkeley have obtained the first 3D structure of a base editor, a promising DNA manipulation tool that can precisely replace one nucleotide with another. This discovery could lead to more versatile and controllable base editors for use in patients, addressing 60% of known genetic diseases.
The study reveals a deep canyon on the SARS-CoV-2 protein complex where viral RNA binding occurs, suitable for inhibitor development. Researchers identified fundamental characteristics of the Nsp16 and Nsp10 protein complex using X-ray crystallography.
The researchers report two new cryo-EM structures representing the pre- and postfusion conformations of the full-length SARS-CoV-2 spike protein. The findings suggest that current vaccine strategies may be relying on limited information about the natural state of the protein, highlighting the need for further evaluation.
Researchers developed ultrathin 'smart nanosheets' that can capture protein complexes from mixtures, enabling faster and more accurate analysis with electron microscopy. This innovation can lead to better understanding of diseases and treatment with drugs.
Physicists at University of Utah pioneered a method to image virus-like particles in real time, revealing the lattice's dynamic nature. The discovery opens up potential new therapies by understanding how Gag and GagPol proteins rearrange, leading to viral maturation.
A study by KAIST researchers used X-ray scattering to track protein folding, revealing multiple forms of an unfolded protein follow different pathways and timelines. The findings could improve computer simulations, paving the way for better disease studies and drug development.
Researchers have solved the structure of a critical protein region in SMCHD1, which plays a key role in 'switching off' genes. The new map reveals how inherited changes in this region cause certain diseases, including muscular dystrophy and developmental disorders.
A $3.3 million NIH grant will fund research into the structure and mechanisms of TDP-43, a protein linked to neurodegenerative conditions like ALS and Alzheimer's disease. The study aims to better understand how post-translational modifications affect TDP-43 assembly and interactions with therapeutic targets.
Scientists have developed a technique to encase protein molecules in a silica shell, preserving vaccine effectiveness even at high temperatures. This technology, known as ensilication, has been proven effective in real-world trials, demonstrating its potential to eradicate vaccine-preventable diseases in low-income countries.
A team of researchers has identified potential new therapeutic targets to treat Parkinson's disease by understanding the structure and dynamics of the protein alpha-synuclein. They found that a specific region of the protein becomes more exposed when it aggregates, which can lead to diseases like Parkinson's.
A new web resource has been created to provide scientists with easy access to the latest SARS-CoV-2 protein structures, ensuring the highest accuracy possible for treatments and vaccines. The tool, developed by an international team of experts, also includes assessments of model quality and enhanced versions when available.
Enzyme structure varies depending on whether it's measured in a test tube or a living cell, according to researchers at the University of Bonn. This fundamental principle has implications for drug research and studies involving biomolecules.
Researchers unveil the structure of a key protein in human metabolism, which could lead to better obesity treatments. The study found that calcium ions play a crucial role in the protein's function, opening new paths for developing targeted pharmaceuticals.
Researchers at Immanuel Kant Baltic Federal University have developed a method for creating vegetable protein non-cholesterol products containing essential amino acids. By optimizing the extrusion process, they improved the texture and taste of meat analogs, making them more comparable to real meat.
Researchers at the University of Leeds have discovered a dynamic shape-shifting mechanism in noroviruses, which may help explain their potent pathogenicity and inform vaccine development. The study's findings could lead to the creation of more effective vaccine candidates using virus-like particles (VLPs).
Researchers at Lund University developed a new imaging method to study protein structures within nerve cells, providing insight into the first molecular changes in neurons affected by Alzheimer's disease. This breakthrough may help explain the mechanisms behind the disease and potentially lead to effective treatments.
The study provides detailed molecular maps of interaction patterns between a GPCR and different G protein subtypes, revealing key features that govern G protein specificity. The sixth transmembrane helix adopts a similar outward shift in the two G protein-bound GCGR structures, forming a common binding cavity to accommodate Gs and Gi.
The Protein Society announced its 2020 award recipients, recognizing leaders and innovators in protein science. Professor Karen Fleming received the Carl Brändén Award for her pioneering work on membrane protein folding, while Professor Stephen Sligar was honored with the Christian B. Anfinsen Award for his development of nanodiscs.
Researchers have unveiled the structure and mechanism of a protein critical to DNA packaging in human cells, which is highly overexpressed in various cancers. The study found that this protein facilitates histone loading by utilizing ATP, offering new insights into developing targeted therapies for cancer treatment.
The study reveals the modular design of ALG6, an enzyme responsible for forming lipid-linked oligosaccharides, enabling its adaptation to various substrates. The researchers also developed methods for synthesizing complex glycans in the lab, providing new insights into LLO biosynthesis.
Researchers have successfully solved the structure of Parkinson's disease-related protein LRRK2 inside cells using a pioneering technique. The study reveals that pathogenic LRRK2 forms exquisitely-organized double-helices around microtubules, suggesting a potential target for therapies.
Scientists have elucidated the mechanism of controlling autophagy through liquid-liquid phase separation, revealing a novel structure responsible for progression. The discovery has significant implications for understanding various intracellular phenomena and developing autophagy-specific control agents.
Researchers are now designing new proteins from scratch with specific functions using computational methods, enabling the creation of novel structures and properties. This breakthrough has significant implications for fields such as vaccine design, targeted drug delivery, and 'smart' therapeutics.
Researchers discovered atomic-resolution structure of BM2, a key influenza B protein. This finding helps design drugs to block the protein and prevent viral spread. The study also revealed unique structural differences between influenza A and B proteins.
Researchers at LMU have determined the structure of a specialized transport system for inserting folded globular proteins into membranes. The system exploits the airlock principle, allowing mitochondria to transfer essential protein Rip1 in its folded state across their inner membrane.
Researchers have identified a unique archaeal protein complex with a five-column tholos-like architecture, featuring a spacious center that can accommodate biomolecules. This discovery provides insight into the molecular evolution between archaeal and eukaryotic proteins.
Researchers from TUM have identified a new role for the alpha-A-crystallin protein in protecting other proteins from oxidation, which may contribute to the prevention of cataracts and age-related blindness. The study reveals that oxidized alpha-A-crystallin can transfer disulfide bridges to other proteins, influencing their redox state.
A new high-throughput method has revealed metals previously undetected in 3-D protein structures, correcting up to half of the errors in global repository of protein structures called PDB.
CryoEM technique reveals structural changes in cardiac muscle thin filaments that regulate heartbeat function. The study provides a molecular basis for novel drug design to treat diseases such as cardiomyopathy.
University of Groningen scientists have successfully reconstructed the ancestral genetic sequences for three FMO genes, revealing the structure of these enzymes and their role in metabolizing toxic substances. The results provide insight into how FMOs work, which could lead to the design of drugs activated by these enzymes.
Researchers have uncovered the near atomic-level structure of a calcium homeostasis modulator, a protein crucial in processing taste stimuli and mitigating brain cell toxicity. This discovery may lead to novel medications for CALHM-related disorders, including Alzheimer's disease and stroke.
A team of researchers at the University of Colorado Boulder has solved the structure of the Facilitates Chromatin Transcription (FACT) protein, a key player in DNA packaging and gene expression. The discovery sheds light on how this protein maintains the integrity of chromatin during transcription, replication, and DNA damage repair.
Researchers solved the three-dimensional structure of potassium chloride cotransporter 1 (KCC1) using cryo-electron microscopy. The study's findings provide new insights into the protein's role in regulating cell volume, particularly in the kidneys and brain, and shed light on potential treatments for hereditary epilepsy.
Scientists develop theoretical structures of the sweet receptor, revealing how proteins work together to signal 'sweet' flavors. The research could lead to improved nutrition and drug development.
A new study shows that X-ray crystallography can provide inaccurate information about critical cell membrane proteins, leading to poor drug design. Researchers used supercomputing to simulate molecular dynamics of a membrane protein and found that unresolved loops can stabilize the protein despite apparent lack of structure.
Researchers create formula to calculate resolution of protein structures based on viewing angles, enabling better methods for imaging proteins. This new approach helps determine the best setup for experiments to improve cryo-EM imaging.
Scientists have created an accurate 3D model of an intrinsically disordered protein using supercomputing and neutron scattering experiments. The ensemble of its atomic-level structures reveals new information about its biological function, including transient ordered structures.
Biological experiments confirm that chromatin in mice eyes changes structure over time, allowing for night vision. Mathematical modeling shows nuclear deformation is a crucial point in DNA's structure change.
A team led by Dr. Lim Hyun-Ho identified a new structure and mechanism of a membrane protein that causes epilepsy and muscle problems. The study reveals four different structures in the ion exchange process for a single CLC protein, expanding our understanding of this protein's functions.
Researchers at Weill Cornell Medicine have illuminated the basic mechanism of Piezo proteins, which function as sensors in the body for mechanical stimuli. The discovery provides insights into the roles of Piezo proteins in human diseases and potential new therapeutic strategies.
Researchers have developed a new 'ubiquitin clipping' technique to study protein modifications, revealing branched ubiquitin chains are common and could impact diseases like cancer and neurodegenerative disorders. The technique enables detailed experimentation, providing insights into disease mechanisms and potential drug targets.
A team of researchers at Ruhr-Universität Bochum has shown that the supposed disorder in the HMGA1a protein is not disorder after all. The protein adopts dynamic, more compact structures that depend on its phosphorylation state. This discovery could lead to new therapeutic strategies for cancers caused by HMGA1a.
Researchers have identified a new mechanism for how plants perceive RALF23 peptides, a key player in regulating important plant processes. The discovery sheds light on how plants respond to internal and external cues, with potential implications for understanding immune defense and development.
Scientists translate amino acid sequences into musical compositions, then use AI to generate new proteins with desired features. The method also enables the creation of bio-based musical pieces.
Protein machines play a crucial role in biological cells, and researchers have developed simple mechanical models to understand their operation. These models, based on elastic networks, reveal essential aspects of protein machine behavior and can be used to design artificial nano-machines with machine properties.
Scientists at the University of Konstanz develop a new method to study the interaction between p53 and poly(ADP-ribose) and DNA, providing insights into molecular reactions to cellular stress and cancer development. The research reveals distinct changes in protein structure induced by these interactions.
Researchers at Harvard Medical School have developed a new method for determining 3D protein structures from lab-designed DNA sequences. By assessing the effects of genetic mutations on protein functions, they were able to identify functional interactions within DNA sequences and construct 3D structures that closely mimicked those deri...
Researchers discovered asymmetrical nuclear pore complex outer ring structures in fission yeast, comprising only two types of Nups, with essential roles in normal cell growth. The findings challenge the long-held assumption that these structures are identical across eukaryotic cells.
Scientists use pattern recognition to understand and predict behavior of disordered strands of proteins and polymers. By analyzing the precise sequence of charged monomers, researchers can design new materials with improved properties.
Scientists have successfully determined the high-resolution three-dimensional structure of proteins inside living eukaryotic cells. This breakthrough technique promises insight into disease-causing proteins and novel drug screening applications.
A study has revealed the structure of FoxM1 protein in its inactive state, which could lead to the development of new cancer treatments by stabilizing the protein. This understanding also provides insight into how transcription factors function and switch between active and inactive states.
Anne Villeneuve, PhD, receives the 2019 Genetics Society of America Medal for her groundbreaking research on meiosis and chromosome inheritance. Her work has significantly impacted our understanding of major aspects of the meiotic program.
A Harvard Medical School scientist has developed a new approach using deep learning to predict protein structure from amino acid sequence. This method achieves accuracy comparable to current state-of-the-art methods but at speeds upward of a million times faster.
A team of scientists has discovered that the neuronal transport factor Staufen2 scans and binds to its target transcripts in a more complex manner than previously thought. This finding opens up new approaches to improve our understanding of RNA transport and synaptic plasticity, which is essential for memory and learning.
Researchers successfully created self-assembled structures using oppositely charged synthetic proteins, enabling the formation of hierarchical ordered, symmetrical structures. This breakthrough could lead to the development of novel architectures for bio-enabled sensing and functional coatings with unique properties.
Researchers develop a method for predicting protein functions using amino acid sequences, eliminating the need for structural data. This breakthrough enables better protein engineering and design, with potential applications in drug development and biological research.
Researchers at UT Southwestern Medical Center used cryo-electron microscopy to determine the near-atomic structure of the smallest membrane protein solved to date. The study reveals new insights into the primitive function of the cGAS-STING pathway, which could lead to better immunotherapies for cancer and autoimmune diseases.
Researchers at the European Molecular Biology Laboratory developed methods to study protein structures under force, revealing a protein 'strain absorber' that stretches up to 2.5 times its original length. This discovery opens new avenues for understanding molecular elasticity in proteins and their response to small forces.