Scientists discovered a common viral harpoon protein structure among measles, mumps and respiratory syncytial viruses. This finding suggests that these viruses may be related to HIV, influenza and Ebola viruses, potentially leading to the development of new drugs.
Scientists Nori Yamaguchi and Harry Gibson have developed a reversible process to form supramolecular polymers, which can be used to create fibers or transport target molecules. The polymers are formed through hydrogen bonding and can be undone at the molecular level using heat or pH.
Scientists have discovered the molecular structure of ZAG, a protein linked to severe weight loss in cancer patients. The discovery provides crucial insights into how ZAG promotes fat breakdown, paving the way for potential treatments for clinical obesity and related conditions.
Researchers at New York University have successfully constructed a machine from synthetic DNA molecules, featuring two rigid arms that can be rotated between fixed positions. This achievement marks a significant step towards developing nano-robots and molecular manufacturing capabilities.
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Researchers have determined the first structure of a functional protein unit involved in neurofibromatosis, which regulates Ras and contributes to tumor growth. The study confirms mechanistic ideas about neurofibromin's function and links NF1 to cancerogenesis.
The study reveals human beta-tryptase is a ring-like tetramer with active sites facing a central pore. Its unique architecture explains many of its distinct biochemical properties and will facilitate understanding of its role in health and disease.
Researcher Robert Connelly uses tensegrities to model molecular structures like buckminsterfullerenes, which have unique geometric stability. His work provides insights into the behavior of certain-shaped molecules and could lead to a catalogue of stable tensegrity structures.
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Scientists at UC Berkeley designed a protein that toggles between two structures upon binding a small molecule, enabling detection of carcinogens like benzene. The newly designed protein could also be used as a molecular switch or zipper to join proteins together.
Researchers use extreme X-ray power to 'movie' myoglobin protein, resolving decades-old structure-function riddle. This breakthrough enables drug developers to design better drugs by understanding dynamic molecular interactions.