The Biophysical Society has announced the winners of its 2010 International Travel Awards, fostering interaction between American biophysicists and scientists in financially difficult countries. The recipients, chosen based on scientific merit, will present their work at the society's Annual Meeting in San Francisco.
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Researchers computationally and experimentally discovered molecular pathways for proteins to change shape without unfolding. They found that proteins follow transient, bridging states lasting less than a nanosecond, enabling function while avoiding unfolding.
Researchers developed a universal method to analyze complex networks, including social networks, protein-protein interactions, and air transportation networks. The method accurately predicts missing and spurious connections by averaging all possible groupings of nodes, giving each grouping a weight that reflects its explanatory power.
Researchers discovered that proteins locate genetic information in DNA by sliding down the double helix, like traveling along a screw. This finding validates a recent theory and could lead to new ways to alter DNA-binding protein behavior.
Scientists have observed ion channels within the surface membrane of cells for the first time, improving our understanding of how signals travel among neurons. This discovery may lead to a complete picture of how ion channels function and could have implications for future drug development.
The studies used molecular dynamics flexible fitting (MDFF) to examine the interaction of the ribosome with EF-Tu and SecY, respectively. The researchers found structural evidence that when the ribosome recognizes the correct tRNA, it induces a change in the shape of EF-Tu, allowing chemical interactions to lead to protein assembly.
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Researchers at Virginia Tech have discovered novel molecular interactions at the surface of platelets that regulate blood clotting. The study found that sulfatides bind to Disabled-2 protein, preventing it from inhibiting clotting, while also recycling the protein for future use.
Scientists discover GM1-ganglioside builds up in brain cells of patients with GM1-gangliosidosis, disrupting calcium balance and leading to programmed cell death. The study suggests a two-step process and identifies key proteins involved in the disease.
Researchers discovered that Stapled Peptides can potently and directly inhibit the Notch transcription factor complex, preventing cancer cell proliferation and survival. The findings validate the potential of Stapled Peptides to modulate key intracellular biological targets.
Scientists discovered how plant hormone ABA interacts with protein PYR1 to trigger drought response. This interaction enables PP2C molecules to be hijacked, allowing plants to increase water uptake and storage while decreasing water loss. The study offers new approaches for increasing crop tolerance to water shortages.
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Researchers at the University of Illinois have discovered a way to fine-tune the reduction potential of copper-containing proteins, enabling the creation of efficient water-soluble redox agents. This breakthrough allows for greater control over electron-transfer properties and extends the range of redox potentials.
Researchers have discovered how critical proteins for eye lens transparency are sorted and concentrated in membrane bilayers. The study reveals that protein-lipid interactions play a key role in this process, with aquaporin clustering influencing its localization in lens cell membranes.
Researchers at Johns Hopkins Medicine have identified over 300 proteins that control genes, a newly discovered function for previously known proteins. These 'moonlighting' molecules may play a key role in human complexity, with potential implications for understanding gene regulation and cellular behavior.
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A team of researchers at the University of Pennsylvania School of Medicine has identified a small molecule that inhibits heat shock protein HSP70, which is overexpressed in tumor cells. The inhibitor, called PES, blocks HSP70's stress-relieving functions and induces cell death by disrupting autophagy.
A new study reveals that a single-stranded DNA-binding protein (SSB) moves back and forth along single-stranded DNA, gradually allowing other proteins to repair, recombine or replicate the strands. SSB's dynamic movement is independent of the DNA sequence and modulates the activity of critical DNA repair proteins.
Researchers have visualized the ribosome's assembly line gears, capturing the intricate interactions between elongation factor G and the ribosome. The study reveals new insights into how EF-G moves the assembly line forward, paving the way for understanding viral hijacking and antibiotic resistance.
Researchers at UC San Diego discover that a protein interaction generates force that shapes the Golgi apparatus, revealing a link between form and function. The discovery sheds light on the mechanism of the Golgi apparatus, a processing center for protein export.
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Scientists have developed a revolutionary technology to analyze protein mixtures, revealing a key enzyme that stabilizes proteins in mitochondria. This breakthrough has significant implications for fundamental research on proteins and their roles in cell function.
Intracellular pathogens like Chlamydia and Legionella exploit host cell biology to escape destruction. Researchers found that SNARE-like proteins expressed by the bacteria inhibit membrane fusion with lysosomes, allowing them to remain in cells.
Researchers can access optimized methods for RNA isolation, qRT-PCR, and coimmunoprecipitation of RNA-protein complexes from zebrafish and C. elegans. These protocols enable the study of RNA interactions with proteins to drive cellular activities.
The NIH has awarded $45 million to four new Centers of Excellence in Genomic Science, including two new centers and two existing ones. The new centers will focus on psychiatric disorders and gene regulation, while the existing centers will continue to advance genomic research. Researchers at the University of North Carolina, University...
Researchers created a complete model of the bacterium Thermotoga maritima's central metabolic network, including three-dimensional protein structures. This breakthrough could help identify positive and adverse drug reactions and engineer bacteria to produce clean energy.
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Scientists have used single-molecule techniques to study the tethered lactose repressor protein, revealing how flexibility within the protein influences its ability to form DNA loops. The results suggest that limiting flexibility limits protein function in this case.
Researchers created a comprehensive model of the bacterium's central metabolic network, including protein structures and interactions. The study reveals essential protein shapes and connections to unique metabolites.
The Biophysical Society has recognized ten new fellows for their exceptional contributions to the field of biophysics. These researchers have made significant advances in understanding the structure and function of biological macromolecules, membrane proteins, and biomembranes through innovative approaches and pioneering techniques.
The article presents optimized ChIP protocol for mammalian cells, while recombineering methods are used to construct targeting vectors for conditional knockout mice. These techniques provide efficient and precise genetic modifications.
A team of researchers from The Wistar Institute have shown that a large non-coding RNA in mammals and yeast plays a central role in helping maintain telomeres. Manipulating this RNA's expression may be useful in treating cancer and other diseases.
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A study published in the journal Genetics identified five new proteins necessary for memory, providing insight into fragile X mental retardation. The researchers used an artificial system to analyze the eye deformities caused by overexpression of a key protein, revealing that each protein is required for its function.
Researchers designed synthetic protein-like mimics that interrupt HIV's interaction with host cell proteins, blocking infection. The novel molecules, dubbed 'foldamers,' are highly resistant to degradation and have potent antiviral activity.
Researchers at Carnegie Institution's Department of Plant Biology have cloned genes for membrane proteins that regulate nutrient and water fluxes in cells. The donated clones will help unravel the interaction of these proteins across species, with potential applications in understanding kidney diseases and engineering better crops.
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Scientists at the University of Georgia have created a two-step computer simulation using the Wang-Landau algorithm to study how glycophorin A folds into its functional shape. The research reveals that the process is driven by a subtle interplay between multiple types of interactions, providing insights into membrane protein folding.
Researchers have discovered that HIV hijacks the autophagy process to facilitate viral replication and survival. By leveraging this cellular pathway, the virus can evade degradation and complete its maturation process.
Researchers at the University of Oregon have discovered a new class of self-assembling materials that can control colloidal interactions by applying biological molecules from cell membranes. The findings suggest that specially tweaked biological membranes can serve as control knobs to direct materials to specific actions.
A K-State researcher is studying protein interactions in the lens of the eye to understand how they trigger cataracts. The goal is to screen drugs that can inhibit or reverse abnormal processes causing cataracts, potentially leading to a nonsurgical method for restoring sight.
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A rapid and inexpensive drug-screening method developed by Whitehead Institute scientists uses baker's yeast to synthesize and screen molecules, cutting testing time to weeks. The technique targets protein-protein interactions found in cellular processes, offering new potential for treating diseases like Parkinson's.
Researchers at GUMC discovered a small molecule that prevents the fusion protein responsible for Ewing's sarcoma from binding to another protein, RNA helicase A. This novel approach could provide a model for designing treatment for other disorders caused by protein-protein interactions.
A team of researchers at the Salk Institute has discovered a specific site within an ion channel protein where alcohols directly interact, altering brain cell communication. This finding could lead to novel treatments for alcoholism, drug addiction, and epilepsy.
Researchers at EMBL have produced a three-dimensional reconstruction of immature HIV, showing its protein coat assembly in unprecedented detail. The study suggests a simple model of HIV formation, involving multiple Gag proteins interacting to form a hexameric lattice.
The SIB Swiss Institute of Bioinformatics awarded Lukas Burger for his innovative Bayesian network methodology for predicting protein sequences. Julien Roux won the award for his paper on vertebrate genome evolution, which challenged the traditional 'hourglass' model by revealing a strong effect of constraints in early development.
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The review article examines various ways nanomaterials interact with biological systems, highlighting the importance of understanding physical and chemical properties for safe use. It presents a roadmap for designing nanoparticle drug-delivery systems with targeted delivery and reducing potential hazardous interactions.
Researchers have developed a new crosslinking method called TRAP to study protein interactions in living cells. The method uses small crosslinkers that can be controlled with light to identify proteins working together, revealing new details about RNA polymerase in bacteria.
Scientists have revealed the structure of the HIV protein shell, providing a close-up look at its unique honeycomb arrangement. The discovery may help identify new ways to block HIV infection and develop novel therapeutic strategies.
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Researchers at Johns Hopkins have discovered a tiny protein called Rhes responsible for brain cell damage in Huntington's disease. The findings explain the unique pattern of brain damage and offer a strategy for new therapy.
Researchers at the University of Michigan have developed small molecules that mimic the behavior and function of a natural regulator of gene expression, binding to a key protein and promoting gene activity. This breakthrough could lead to new approaches for treating diseases caused by errors in gene regulation.
A study by Fox Chase Cancer Center researchers reveals that 'disordered' amino acids in the signaling protein NHERF1 enable flexibility and molecular switching. This finding challenges traditional views on the role of disordered sequences in proteins.
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Researchers at Medical College of Georgia have identified a critical protein called erbin that regulates insulation in the peripheral nervous system. Impaired myelin formation is linked to neurological and psychiatric diseases, while erbin's role in cancer therapy provides a potential new site for targeted treatment.
A team of scientists has identified the molecular structure of hemocyanin, a protein complex involved in skin and hair coloring. The study reveals how hemocyanin is activated, leading to an understanding of both albinism and melanoma.
Researchers found that antibody interference can hinder vaccine effectiveness, proposing a new approach to design more powerful vaccines. They suggest intentionally developing a vaccine strain that differs from the anticipated infectious virus at specific sites.
A team of scientists discovered a genetic modifier, A229T, that increases the risk of retinal degeneration and blindness in patients with ciliary diseases. The study found that this change affects protein interactions critical for retinal function, leading to progressive vision loss.
Researchers at EMBL and PSI create ACEMBL, a new technology that produces multiprotein complexes with reduced effort and materials, speeding up structural studies and deciphering molecular mechanisms of health and disease. The system will be adapted for eukaryotic cells to study human origins and complex drug targets.
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Researchers identify cowpea mosaic virus's target protein vimentin, a key step towards using the virus as a drug delivery agent. The discovery may lead to targeted treatment of tumors and potentially prevent infectious diseases.
A study published in the Journal of Biological Chemistry reveals a novel protein called RANBP9, which when over-expressed leads to increased generation of amyloid-beta peptide. The researchers found that inhibiting RANBP9 may offer an alternative approach to therapy for Alzheimer's disease.
Researchers have identified 39 interaction partners of bacterial toxins, revealing how these toxins manipulate human host cell signaling pathways. This breakthrough could lead to the development of new treatments targeting the underlying mechanisms disrupted by bacterial toxins.
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Researchers at the Institute of Bioengineering and Nanotechnology have synthesized gold nanoclusters that can be used for sub-cellular biolabeling and bioimaging. These clusters are suitable for use within the body due to their lack of toxic metals, enabling scientists to monitor cell nucleus dynamics and study genomic changes.
A team of scientists has identified a crucial requirement for heterochromatin formation, showing that the strength of Chp1's binding to methylated chromatin is essential. This breakthrough reveals a key mechanism in regulating gene expression and genomic stability.
Researchers at Duke University Medical Center have identified a signaling pathway that initiates the flushing response associated with nicotinic acid. Analysis of human cell lines revealed that beta-arrestin proteins play a key role in this process, which may be targeted to prevent side effects while maintaining therapeutic benefits. I...
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Biomedical engineers have developed a new probe that allows visualization of single RNA molecules within live cells, enabling scientists to study RNA's operation and interaction with binding proteins. The tool overcomes issues with fluorescent probes, allowing for hours-long imaging and distinguishing between targeted and unbound probes.
New Brown University research suggests nicotine interferes with multiple cellular interactions, potentially developing new treatments for various diseases. The study identified 55 proteins interacting with the alpha-7 nicotinic receptor, which may have broader roles in the body than previously thought.
A Scripps Research team discovered peptides that inhibit viral production by 68-63% and reduce viral RNA levels by sevenfold. The findings offer a promising target for the development of anti-hepatitis C virus drugs.
Researchers have determined the structure of a protein within its natural environment, Escherichia coli, for the first time using nuclear magnetic resonance (NMR) spectroscopy. This milestone advances our understanding of molecular biology and opens new avenues for investigating protein interactions in living systems.