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Novel calculations have enabled the study of nearly 700 isotopes between helium and iron, showing which nuclei can exist and which cannot. In an article published in Physical Review Letters, scientists from TU Darmstadt, the University of Washington, the Canadian laboratory TRIUMF, and the University of Mainz report how they simulated for the first time using innovative theoretical methods a large region of the chart of nuclides based on the theory of the strong interaction
Atomic nuclei are held together by the strong interaction between neutrons and protons. About ten percent of all known nuclei are stable. Starting from these stable isotopes, nuclei become increasingly unstable as neutrons are added or removed, until neutrons can no longer bind to the nucleus and 'drip' out. This limit of existence, the so-called neutron 'dripline,' has so far been discovered experimentally only for light elements up to neon. Understanding the neutron dripline and the structure of neutron-rich nuclei also plays a key role in the research program for the future accelerator facility FAIR at the GSI Helmholtz Centre for Heavy Ion Research in Darmstadt.
In a new study, "Ab Initio Limits of Nuclei," published in the journal Physical Review Letters as an…
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Ribosomes are the complexes of ribonucleoproteins at the heart of protein synthesis in cells. However, in the absence of conclusive evidence, how these complexes operate has been open to debate. Now, Hirotatsu Imai and Noriyuki Kodera at Kanazawa University, alongside Toshio Uchiumi at Niigata University in Japan, show visualizations of the structural dynamics and factor pooling that take place at ribosome stalk proteins as they build new proteins
Ribosomes were first discovered in the 1950s, and their broad function has been widely understood for some time—they read messenger RNA sequences, and from that, generate sequences of correctly ordered amino acids into new proteins. The ribosome stalk protein in particular plays an integral role in the protein synthesis process by recruiting protein factors responsible for translation and elongation of the amino acid sequence. However, it has been hard to establish the structure of the bound ribosome stalk protein because of its flexibility. Here, the high resolution and fast image capture of high-speed atomic force microscopy proved invaluable.
Atomic force microscopy uses a nanoscale tip to trace the samples, much like a vinyl record player needle scanning over a record, except that the details identified by an atomic force microscope can have…