Researchers analyzed X-ray crystal structures of resurrected Precambrian proteins, revealing structural similarity among proteins since life first evolved on Earth. This approach provides insights into protein structure evolution and may aid in designing novel proteins.
Researchers at the University of Pennsylvania designed a variant of the mu opioid receptor, which can be grown in large quantities in bacteria and is water-soluble, enabling experiments that were previously challenging or impossible. The new design allows for further iterations to be easily made alongside experimental conditions.
SourceUniversity of Pennsylvania·JournalPLOS ONE·DateJun 14, 2013
A novel avian-origin H7N9 influenza virus was found to show rapid evolution, with several viruses circulating in Hangzhou. The virus's pathogenesis in humans remains unknown, but substitutions have been identified as potential pathogenicity factors.
Researchers at Johns Hopkins Medicine found that the location of rhomboid proteases within membranes enables them to recognize and cut unstable proteins. This discovery has profound implications for understanding diseases like Alzheimer's and developing treatments.
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Researchers developed a new method called HHblits that surpasses PSI-BLAST in performance by increasing sensitivity and precision. By analyzing similar sequences, scientists can infer the structure and functions of proteins more accurately and frequently than before.
SourceLudwig-Maximilians-Universität München·JournalNature Methods·DateDec 25, 2011
Studies using single-molecule fluorescence reveal that neighboring protein domains with similar amino acid sequences are more prone to misfold, potentially leading to neurodegenerative diseases. This finding suggests that proteins have evolved to limit similarity between domains to prevent misfolding and maintain functionality.
Researchers at UCLA have made a breakthrough in controlled engineering of nanocatalysts by using surfactants and biomolecules to produce predictable shapes. This innovation has the potential to improve catalytic properties and lead to more efficient energy production and reduced pollution.
SourceUniversity of California - Los Angeles·JournalNature Chemistry·DateApr 19, 2011
Researchers isolated an enzyme from Arabidopsis thaliana that catalyzes glucosinolate formation and found it resembles an enzyme involved in leucine synthesis. This structural similarity enabled the plant to produce toxic compounds as a defense mechanism, highlighting the importance of small genetic changes in evolutionary adaptations.
SourceMax Planck Institute for Chemical Ecology·JournalThe Plant Cell·DateMar 17, 2011
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Researchers at Arizona State University have developed synthetic antibodies that can be used for diagnostic tools. By optimizing binding affinity using random peptide sequences, these synbodies show promise in detecting diseases early on.
SourceArizona State University·JournalPLOS ONE·DateJan 24, 2011
Researchers use temperature jump and fast chemical reaction to capture protein folding process, providing detail needed for accurate predictions. The new method offers hope for improving protein structure predictions, which are crucial for medicine and biotechnology.
SourceWashington University in St. Louis·JournalJournal of the American Chemical Society·DateJan 10, 2011
Researchers create genetic sequences never seen in nature and produce substances sustaining life in cells almost as readily as natural proteins. The team's work represents a significant advance in synthetic biology, suggesting the construction of artificial genomes capable of sustaining cell life may be within reach.
SourcePrinceton University·JournalPLOS ONE·DateJan 6, 2011
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.
SourceTechnical University of Munich (TUM)·JournalNature·DateOct 27, 2010
Researchers at Arizona State University have developed a method to create synthetic antibodies that can bind with human proteins with high affinity and specificity. This technique, called synbody construction, involves combining random amino acid sequences to form a binding molecule that can target specific proteins.
SourceArizona State University·JournalPLOS ONE·DateMay 19, 2010
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Researchers discovered that adding proline and phenylalanine amino acids improves binding rates of synthetic fibrin knobs to holes, leading to a novel peptide mimic with 10-fold higher affinity. The study also identified structural properties contributing to functional knob-hole interactions.
SourceGeorgia Institute of Technology·JournalBlood·DateMay 19, 2010
A new study by researchers at the University of Michigan found that echolocating bats and whales share a similar molecular mechanism for this ability, overturning conventional thinking on convergence. The research focused on the prestin gene, which plays a crucial role in hearing and amplifying sounds.
SourceUniversity of Michigan·JournalCurrent Biology·DateJan 25, 2010
Researchers discover unique structure in viral protein Rev, allowing it to penetrate nucleus and nucleoli. This finding opens new avenues for studying the relationship between protein localization and host cell impact.
SourceUniversité du Québec à Montréal·JournalJournal of Virology·DateJan 5, 2010
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A team of Penn biochemists designed a simple and robust oxygen-transporting protein using design principles inspired by nature. They successfully created the protein, which can transport oxygen, using a set of simple design principles.
SourceUniversity of Pennsylvania School of Medicine·JournalNature·DateMar 23, 2009
Researchers Johannes Soeding and Andreas Biegert have developed a new method called CS-BLAST that takes into account the sequence context to improve similarity searches. This approach can identify twice as many distant relatives of proteins compared to traditional BLAST, leading to better insights into gene and protein functions.
SourceLudwig-Maximilians-Universität München·JournalProceedings of the National Academy of Sciences·DateFeb 23, 2009
Researchers have developed a new method to reconstruct the evolutionary history of the HIV-1 V3 loop, revealing biologically dependent amino acids that form 'co-evolving' ties across the protein. This study advances understanding of HIV-1 evolution and identifies potential targets for future research.
SourcePLOS·JournalPLOS Computational Biology·DateNov 23, 2007
Researchers discovered that abnormal glutamine repeats interfere with key transcription factor TBP, leading to neurodegeneration in PolyQ diseases. The study provides insight into the molecular mechanisms underlying these inherited disorders.
SourceEmory Health Sciences·JournalNature Neuroscience·DateNov 13, 2007
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Scientists have developed a novel approach to probing protein folding energy, revealing the slope and height of the energy barrier proteins must overcome. This method has the potential to shed light on how amino acid sequences affect protein function and how diseases arise from misfolding.
SourceRice University·JournalPhysical Review Letters·DateJul 19, 2007
A team of researchers has developed a computational approach to accurately predict the function of proteins with unknown structures and functions. By comparing amino acid sequences to known proteins, they can identify potential substrates and understand the protein's biological role.
SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalNature Chemical Biology·DateJul 11, 2007
Researchers at Arizona State University have evolved new proteins in a fraction of the time it took nature, providing new lessons on how to optimize proteins. The team used 'synthetic evolution' to improve protein stability and binding efficiency, discovering that subtle amino acid changes can significantly enhance function.
SourceArizona State University·JournalPLOS ONE·DateMay 22, 2007
A team of scientists led by Dr. Mary Schweitzer confirmed the presence of original protein fragments in soft tissue from a 68 million-year-old Tyrannosaurus Rex fossil. The discovery uses mass spectrometry to analyze ancient proteins, providing new insights into fossil preservation and potential medical applications.
SourceNorth Carolina State University·JournalScience·DateApr 12, 2007
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Researchers have successfully sequenced tiny pieces of collagen protein from a 68 million-year-old Tyrannosaurus rex fossil, closely matching amino acid sequences found in present-day chickens. The findings support the long-debated proposal that birds and dinosaurs are evolutionarily related.
SourceHarvard Medical School·JournalScience·DateApr 12, 2007
Recent breakthroughs have enabled researchers to construct an atom-by-atom model of the ribosome, a complex molecular machine responsible for synthesizing proteins. The high-resolution images reveal detailed interactions between the ribosome, messenger RNA, and transfer RNAs, providing new insights into protein synthesis.
SourceUniversity of California - Santa Cruz·JournalCell·DateSep 13, 2006
Researchers found that a slight difference in protein shape allows dioxin to bind more easily, triggering harmful effects. A test using molecular analysis could help assess dioxin sensitivity in wild animal populations.
SourceWoods Hole Oceanographic Institution·JournalProceedings of the National Academy of Sciences·DateMay 18, 2006
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A new study by researchers at Case Western Reserve University has found that an abnormal form of the prion protein from one mammal species can infect another species, bypassing natural barriers. This discovery sheds light on the mechanisms behind prion diseases like mad cow disease and Creutzfeldt-Jakob disease.
SourceCase Western Reserve University·JournalMolecular Cell·DateApr 8, 2004
Scientists have identified amino acid sequences that allow prions to aggregate and replicate, leading to the creation of an artificial yeast prion. This breakthrough sheds light on the mechanisms behind diseases like mad cow disease and Alzheimer's, potentially paving the way for new treatments.
Scientists successfully designed and built an artificial protein using a novel computational approach, opening up new possibilities for medicine and industrial applications. The achievement represents a significant breakthrough in understanding protein folding and design.
SourceHoward Hughes Medical Institute·JournalScience·DateNov 20, 2003
Researchers at UCSD have identified two peptide sequences that bind to abnormal beta-amyloid plaques in Alzheimer's disease. The peptides may be used for diagnostic tests or coupled with molecules to inhibit plaque toxicity, making them a promising new approach to the disease.
SourceUniversity of California - San Diego·JournalNeurobiology of Disease·DateSep 8, 2003
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Researchers use high-speed imaging to track movement of calcium waves in cell signaling, identifying a sequence of amino acids (LTL) that controls the pathway. The findings have implications for treating autoimmune diseases such as arthritis and uveitis.
SourceMichigan Medicine - University of Michigan·JournalProceedings of the National Academy of Sciences·DateApr 16, 2003
Researchers will use computational biolinguistics to analyze protein sequences and understand their structure, dynamics, and function. This project aims to extract information from gene sequences that may lead to developing drugs to fight degenerative diseases.
Researchers at JCI Journals have made significant strides in understanding the biological function and clinical relevance of copolymers. The study's findings hold promise for developing new treatments for various human diseases.
SourceJCI Journals·JournalJournal of Clinical Investigation·DateJun 12, 2002
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Scientists have identified a protein segment responsible for fibrous tissue growth leading to liver cirrhosis. They've developed a mutated version of the protein that blocks this process in mice, offering potential new hope for treating liver diseases.
SourceUniversity of California - San Diego·JournalMolecular Cell·DateOct 25, 2001
Researchers at Brown University have developed a new way to sequence DNA that is faster and more efficient than current methods. By inserting gaps into DNA probes, they can extract substantially more information about the DNA, allowing for the sequencing of tens of thousands of bases.
Scientists create first bi-directional molecular motor by changing a single amino acid, disrupting the sense of direction in another. The discovery opens up new possibilities for understanding diseases caused by incorrect chromosome distribution during cell division.
SourceDuke University Medical Center·JournalNature·DateAug 22, 2000
Scientists from Max Planck Institute report correlation between impaired RNA editing and epilepsy. Genetic manipulation in mice reveals that correcting the defect can lead to improved brain function and reduced seizures. The study suggests a potential link between human genome sequence and neurological disorders.
SourceMax-Planck-Gesellschaft·JournalNature·DateJul 5, 2000
Researchers have identified a structural anomaly in the Taq DNA polymerase enzyme that hampers its performance in DNA sequencing. By modifying this anomaly, scientists created an improved version of the enzyme, which increases sequencing speed and reduces errors.
SourceWashU Medicine·JournalProceedings of the National Academy of Sciences·DateAug 17, 1999
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Researchers at University of Wisconsin-Madison found that amino acids must attach to transfer RNA (tRNA) in the nucleus for efficient delivery out of the nucleus. This quality-control process, known as proofreading, ensures genetic instructions are complete and ready to function.
SourceUniversity of Wisconsin-Madison·JournalScience·DateDec 10, 1998
Researchers have developed molecular sensors that can detect specific proteins in blood plasma or other biological fluids with high accuracy. The sensors could also be used to construct an environmental detector, giving new insights into cell functioning and promoting medical diagnostics.
SourceColumbia University·JournalScience·DateFeb 6, 1998
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.