A simple interpretation of quantum mirages

In an interesting new experiment the electronic structure of a magnetic atom adsorbed on the surface of Cu(111), observed by STM, was projected into a remote location on the same surface. The purpose of the present paper is to interpret this experiment with a model Hamiltonian, using ellipses of the size of the experimental ones, containing about 2300 atoms. The charge distribution for the different wavefunctions is analyzed, in particular, for those with energy close to the Fermi energy of copper Ef. Some of them show two symmetric maxima located on the principal axis of the ellipse but not necessarily at the foci. If a Co atom is adsorbed at the site where the wavefunction with energy $E_F$ has a maximum and the interaction is small, the main effect of the adsorbed atom will be to split this particular wavefunction in two. The total charge density will remain the same but the local density of states will present a dip at Ef at any site where the charge density is large enough. We relate the presence of this dip to the observation of quantum mirages. Our interpretation suggests that other sites, apart from the foci of the ellipses, can be used for projecting atomic images and also indicates the conditions for other non magnetic adsorbates to produce mirages.Comment: 3 pages, 3 Fig

A human testicular teratoma serially transplanted in immune-deprived mice.

Serial transplantation of an HCG-producing human testicular teratoma in immune-deprived mice is described. The xenografted tumour was compared to the tumour of origin in histology, immunohistochemistry (using an immune peroxidase technique to localize HCG) autoradiography, marker production and growth rate. It is concluded that the xenograft retained the characteristics of the original tumour with the exception of a reduction in HCG-producing elements at transplantation beyond 5 serial passages

Myosin tails and single α-helical domains

The human genome contains 39 myosin genes, divided up into 12 different classes. The structure, cellular function and biochemical properties of many of these isoforms remain poorly characterized and there is still some controversy as to whether some myosin isoforms are monomers or dimers. Myosin isoforms 6 and 10 contain a stable single α-helical (SAH) domain, situated just after the canonical lever. The SAH domain is stiff enough to be able to lengthen the lever allowing the myosin to take a larger step. In addition, atomic force microscopy and atomistic simulations show that SAH domains unfold at relatively low forces and have a high propensity to refold. These properties are likely to be important for protein function, enabling motors to carry cargo in dense actin networks, and other proteins to remain attached to binding partners in the crowded cell