Articles tagged with Protein Structure
A new study published in ACS' Journal of Agricultural and Food Chemistry found that sous vide cooking increases beef protein digestibility compared to boiling or roasting. Sous vide cooking produced less protein oxidation and aggregation, releasing a greater quantity and variety of peptides.
A novel method detects conformational changes in TDP-43 protein in ALS patients' CSF, showing high sensitivity and specificity. The technology has potential for diagnosing and developing clinical therapies for this fatal neurodegenerative disease.
Researchers have developed new computational tools to speed up molecular dynamics simulations, enabling novel studies on protein behavior. The tools are being used to predict the 3D shape of unknown proteins in COVID-19 viruses, which could lead to new drug developments.
Researchers from Heidelberg University Biochemistry Center have determined the 3D structure of a molecular machine responsible for correctly placing tail-anchored membrane proteins into biomembranes. This finding provides crucial insights into protein transport and insertion, shedding light on the final steps of the process.
AlphaFold's breakthrough could accelerate biological research, unlocking new possibilities in disease understanding and drug discovery. The system determines highly-accurate structures in a matter of days, achieving a median score of 92.4 GDT across all targets.
Researchers have made significant progress in determining the shape of proteins, a crucial aspect of understanding diseases. An AI solution, AlphaFold, has demonstrated accuracy comparable to laboratory experiments and has the potential to revolutionize life sciences.
MIT chemists determine the molecular structure of a key coronavirus protein, E, which forms an ion channel that plays a key role in viral replication and inflammation. The study may lead to the development of alternative small molecules that target this channel with high affinity.
The journal CrystEngComm has published a special issue to mark the Cambridge Structural Database's (CSD) milestone, featuring 33 papers showcasing diverse research enabled by the database. The CSD, curated by the CCDC, offers insights into solid-state and crystalline materials, from bond nature to MOF discovery.
Researchers have created a map of the proton-activated chloride channel (PAC), a protein that can help brain cells survive during stroke. Understanding its structure, they hope to develop ways to reduce permanent damage caused by acidosis and improve medical outcomes.
A 3D modeling tool has been created to visualize the components of SARS-CoV-2, ranging from 10 to 100 nanometers in size. The model provides a detailed representation of the virus's structure, including its nucleocapsid proteins and RNA strand.
Fourier transform infrared spectroscopy (FTIR) is widely used for predicting protein secondary structure and quantifying proteins. The technique can detect structural modifications due to interactions with other materials, making it useful for various sample types.
Scientists developed BiteNet, a machine learning algorithm using computer vision to analyze protein structures and detect binding sites. The approach expands the array of possible pharmacological targets and improves speed and accuracy.
The 'nap' protein complex, essential for M. pneumoniae's attachment, movement, and transformation, has been clarified at the atomic level. The study reveals that P40/P90 proteins bind to sialic acid substance on cell surfaces, contrary to popular belief.
A team of researchers has discovered the atomic-level mechanism that governs the length of heart muscle protein filaments, a critical component in maintaining healthy heart function. The study provides new insights into genetic mutations that cause devastating hereditary heart conditions.
Researchers developed a novel grid to minimize sample movement in single-particle cryo-EM, resulting in higher image quality and increased data throughput. The new support film, dubbed 'hexAuFoil,' reduces particle displacement and enables the collection of clearer protein structures.
Researchers at University of Freiburg and University of Zurich provide detailed understanding of allostery's dynamics and structure changes. Allostery is crucial for protein signaling, with disruptions potentially leading to diseases like cancer.
A new algorithm called Ohm predicts allosteric sites in proteins using their structure, which can aid in protein engineering and drug design. The tool may help reduce unintended side effects caused by drugs targeting similar proteins.
Researchers have reconstructed a ciliate mitoribosome using cryo-EM, identifying nine novel proteins encoded in the mitochondrial genome and challenging existing views on mitochondrial translation evolution. The discovery provides new insights into mitochondria's structural and functional complexity.
A team of scientists created a computational model of proteins responsible for transforming mercury to toxic methylmercury, shedding light on how this reaction occurs and its environmental impact. The models suggest that conserved cysteine amino acids in HgcB are involved in shuttling mercury to HgcA during the reaction.
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.
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.
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 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.