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Scientific Highlights

Quantifying Myelin and Axon Orientations in the Brain
Made of a repeated structure of proteins and fats, myelin insulates our nerve cells, allowing signals to travel quickly and efficiently. If myelin is damaged, nervous system signals will not transmit as well. The degree of myelination could be an important diagnostic for brain health because it is disrupted in almost all known brain diseases. Yet current technologies to observe and measure myelin are inadequate for diagnostic applications.
Cross-β Structure - a Core Building Block for Streptococcus mutans Functional Amyloids
Amyloid, composed largely of mis-folded proteins that form insoluble fibrillar aggregates, is important to many human diseases including Alzheimer’s. Tooth decay also features amyloid-forming proteins, but in this case it is not mis-folded human amyloid proteins but bacterial proteins that are not mis-folded when they aggregate into functional amyloid polymers. The most common infectious disease in humans, tooth decay, involves the formation of microbial communities in biofilms on teeth.
Structure of the Full-length Clostridium difficile Toxin B
Clostridium difficile (C. diff) is an opportunistic pathogen that establishes in the colon when the gut microbiota are disrupted, often seen in seriously ill or elderly patients. Clostridium difficile infection (CDI) has become the most common cause of antibiotic-associated diarrhea and gastroenteritis-associated death in developed countries, accounting for a half-million cases and 29,000 deaths annually in the US. It is considered an “urgent threat” by the CDC.
Structural Mechanisms of Histone Recognition by Histone Chaperones
Chromatin is the complex of DNA and proteins that comprises the physiological form of the genome. Non-covalent interactions between DNA and histone proteins are necessary to compact large eukaryotic genomes into relatively small cell nuclei. The nucleosome is the fundamental repeating unit of chromatin, and is composed of 147bp of DNA wrapped around an octamer of histone proteins: 2 copies of each H2A, H2B, H3 and H4.
Synchrotron Small Angle X-ray Scattering Studies Reveal the Role of Neuronal Protein Tau in Microtubule Bundle Formation with Architectures Mimicking those Found in Neurons
Microtubules (MTs) are sub-cellular structures made of the protein tubulin. They have important roles in moving organelles around the cell and in chromosome segregation before cell division. MTs can exist in two states, either a dynamic state of growing and shrinking MTs or a stable state. MTs can also form complex bundles that can be found in neuronal axons. The neuronal protein Tau helps facilitate this process and has been implicated in some neurodegenerative disorders like Alzheimer’s disease. Yet Tau’s exact role in MT formation and bundling is unclear: different experiments (both in vivo and cell free) have shown Tau to mediate either attractive or repulsive forces between MTs.

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