A recently awarded National Institutes of Health (NIH) grant will help integrate existing structural biology resources at the ALS to better serve users. The funds will help establish a centralized collaborative mechanism, called ALS-ENABLE, that will guide users through the most appropriate routes for answering their biological questions. Read more »
The bacterium, H. modesticaldum, is thought to have a photosynthetic reaction center resembling the earliest common ancestor of all photosynthesis complexes. Its molecular structure has now been solved, providing insight into the evolution of photosynthesis and how nature optimized light-driven energy collection. Read more »
Curved β sheets are basic building blocks of many protein cavities that, by serving as binding sites for other molecules, are essential to protein function. β-sheet curvature can now be controlled with atomic-level accuracy, opening the door to custom-designed sites capable of entirely new functions.
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A noncanonical amino-acid (NCAA) complex has been found to drive the self-assembly of a computationally designed protein. Bpy-ala, which is “noncanonical” because it’s not among the 20 amino acids that occur naturally, has useful properties that could be used to generate novel photoactive proteins. Read more »
The structures of proteins controlling calcium-ion transport through cell membranes have been revealed, bound to two drugs known as calcium channel blockers. The discovery might accelerate the development of safer and more effective drugs for treating cardiovascular disorders such as high blood pressure, chest pain, and irregular heartbeat.
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Designed proteins containing hydrogen-bonding modules have been validated by crystallography and SAXS. The ability to design synthetic molecules that combine the specificity of DNA-like binding with protein function opens up huge opportunities for the fields of synthetic biology and materials science. Read more »
Scientists have identified and validated a novel approach to reducing lignin in plants by tweaking a key lignin enzyme. Their technique could help lower the cost of converting biomass into carbon-neutral fuels to power cars and other sustainably developed bio-products. Read more »
Researchers have published a landmark study that used both crystallography and SAXS to validate computationally designed structures of novel proteins with repeated motifs. The results show that the protein-folding universe is far larger than realized, opening up a wide array of new possibilities for biomolecular engineering. Read more »
Scientists working at the ALS recently solved the crystallographic structures of several amine transporters in an effort to better understand why the human brain responds to chemicals like dopamine and serotonin. What they found will help in the design of drugs to treat many neurological diseases, and may also lead to a better understanding of how addiction to abused drugs such as cocaine can be managed. Read more »
Neurotransmitter receptor proteins are critical to learning and memory. Mutations are associated with neurological and neuropsychiatric conditions including Alzheimer’s, epilepsy, and autism. Structures of two such receptors, solved by x-ray crystallography, provide a blueprint for the development of therapeutics.
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