Unbinding Transition Induced by Osmotic Pressure in Relation to Unilamellar Vesicle Formation

Small-angle X-ray scattering and phase-contrast microscopy experiments were performed to investigate the effect of the osmotic pressure on vesicle formation in a dioleoylphosphatidylcholine (DOPC)/water/NaI system. Multi-lamellar vesicles were formed when a pure lipid film was hydrated with an aqueous solution of NaI. On the other hand, uni-lamellar vesicles (ULVs) were formed when a lipid film mixed with an enough amount of NaI was hydrated. To confirm the effect of the osmotic pressure due to NaI, a free-energy calculation was performed. This result showed that the osmotic pressure induced an unbinding transition on the hydration process, which resulted in ULV formation

Orbital Properties of Sr3Ru2O7 and Related Ruthenates Probed by 17O-NMR

We report a site-separated $^{17}$O-NMR study of the layered perovskite ruthenate Sr$_3$Ru$_2$O$_7$, which exhibits nearly two-dimensional transport properties and itinerant metamagnetism at low temperatures. The local hole occupancies and the spin densities in the oxygen $2p$ orbitals are obtained by means of tight-binding analyses of electric field gradients and anisotropic Knight shifts. These quantities are compared with two other layered perovskite ruthenates: the two-dimensional paramagnet Sr$_2$RuO$_4$ and the three-dimensional ferromagnet SrRuO$_3$. The hole occupancies at the oxygen sites are very large, about one hole per ruthenium atom. This is due to the strong covalent character of the Ru-O bonding in this compound. The magnitude of the hole occupancy might be related to the rotation or tilt of the RuO$_6$ octahedra. The spin densities at the oxygen sites are also large, 20-40% of the bulk susceptibilities, but in contrast to the hole occupancies, the spin densities strongly depend on the dimensionality. This result suggests that the density-of-states at the oxygen sites plays an essential role for the understanding of the complex magnetism found in the layered perovskite ruthenates.Comment: 9 pages, 5 figures, to be published in Phys. Rev.

Angle-Resolved Photoemission Spectroscopy of the Antiferromagnetic Superconductor Nd1.87Ce0.13CuO4: Anisotropic Spin-Correlation Gap, Pseudogap, and the Induced Quasiparticle Mass Enhancement

We performed high-resolution angle-resolved photoemission spectroscopy on Nd1.87Ce0.13CuO4, which is located at the boundary of the antiferromagnetic (AF) and the superconducting phase. We observed that the quasiparticle (QP) effective mass around (pi, 0) is strongly enhanced due to the opening of the AF gap. The QP mass and the AF gap are found to be anisotropic, with the largest value near the intersecting point of the Fermi surface and the AF zone boundary. In addition, we observed that the QP peak disappears around the Neel temperature (TN) while the AF pseudogap is gradually filled up at much higher temperatures, possibly due to the short-range AF correlation.Comment: 4 pages, 4 figure

HEAT repeats – versatile arrays of amphiphilic helices working in crowded environments?

Cellular proteins do not work alone in diluted conditions. They often function as part of large macromolecular complexes, which are transported and concentrated into specific cellular compartments and function in their highly crowded environments. A central theme of modern cell biology is to understand how cellular proteins might achieve these challenging tasks efficiently and faithfully. In this Opinion article, we will focus on HEAT repeats, flexible arrays of amphiphilic helices found in many eukaryotic proteins such as karyopherins and condensins, and discuss how this uniquely designed helical repeats might underlie dynamic protein-protein interactions and support cellular functions in crowded environments. We will make bold speculations on functional similarities between HEAT repeats and intrinsically disordered regions (IDRs) in macromolecular phase separation. Potential contributions of HEAT-HEAT interactions, as well as cooperation between HEATs and IDRs, to mesoscale organelle assembly will be discussed