Theoretical models of stellar formation propose the existence of very massive stars that can attain up to 150 times the mass of our Sun.
Until very recently, however, no scientist had discovered a star of more than 83 solar masses. Now an international team of astrophysicists, led by Université de Montréal researchers from the Centre de recherche en astrophysique du Québec (CRAQ), has found and "weighed" the most massive star to date.
Olivier Schnurr, Jules Casoli and André-Nicolas Chené, all graduates of the Université de Montréal, and professors Anthony F. J. Moffat and Nicole St-Louis, successfully "weighed" a star of a binary system with a mass 116 times greater than that of the Sun, waltzing with a companion of 89 solar masses, doubly beating the previous record and breaking the symbolic barrier of 100 solar masses for the first time.
Located in the massive star cluster NGC 3603, the supermassive star system, known under the name of A1, has a rotation period of 3.77 days. The masses were calculated by a combination of observations made with the SINFONI instrument, an integral field spectrograph operating on the Very Large Telescope on the site of the European Organisation for Astronomical Research in the Southern Hemisphere (ESO) in Chile, and infrared images coming from the Hubble Space Telescope.
The stars forming the A1 system are so massive and bright that the light they transmit shows characteristics that only "Wolf-Rayet" stars possess. Within the context of this work, a binary system transmitting X-rays at a power almost never seen in our Galaxy was also discovered near NGC 3603-A1.
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Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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