Spin-orbit coupling has proven indispensable in realizing topological materials and more recently Ising pairing in two-dimensional superconductors. This pairing mechanism relies on inversion symmetry breaking and sustains anomalously large in-plane polarizing magnetic fields whose upper limit is expected to diverge at low temperatures, although experimental demonstration of this has remained elusive due to the required fields. In this work, the recently discovered superconductor few-layer stanene, i.e. epitaxially strained -Sn, is shown to exhibit a new type of Ising pairing between carriers residing in bands with different orbital indices near the Γ-point. The bands are split as a result of spin-orbit locking without the participation of inversion symmetry breaking. The in-plane upper critical field is strongly enhanced at ultra-low temperature and reveals the sought for upturn.

Vortex shedding from flat plates with square leading and trailing edges having chord-to-thickness ratios 3–16 at Reynolds numbers (1–3) × 103 is investigated experimentally in low-speed wind tunnels. It is shown that vortex shedding from flat plates with square leading and trailing edges is characterized by the impinging-shear-layer instability where the separated shear layer becomes unstable in the presence of a sharp trailing edge corner. The Strouhal number which is based on the plate's chord is approximately constant and equal to 0.6 for chord-to-thickness ratios 3–5. With further increase in the ratio it increases stepwise to values that are approximately equal to integral multiples of 0.6.

We previously reported a new brain‐specific protein with a molecular mass of 14 kDa, specifically present in synapses around neurons but not in glial cells [Nakajo, S., Omata, K., Aiuchi, T., Shibayama, T., Okahashi, I., Ochiai, H., Nakai, Y., Nakaya, K. & Nakamura, Y. (1990) J. Neurochem. 55, 2031–2038]. In the present study, we determined the primary structure of this protein, found that it is phosphorylated in vitro and in vivo, and designated it phosphoneuroprotein 14 (PNP 14). The protein is a single polypeptide with 134 amino acid residues (molecular mass = 14122Da), and it contains a hydrophobic region at the center of the molecule. The carboxy‐terminal region has all seven proline residues, and is rich in glutamic acid, which contribute to the acidic property of the protein. The amino‐terminal region possesses four unique repetitive motifs, Glu(Ser)‐Lys‐Thr‐Lys‐Glu(Gln)‐Gly(Gln)‐Val(Ala). When a cytosolic fraction prepared from rat cerebral cortex was incubated with [γ−32P]ATP, 32P was incorporated into PNP 14. Phosphorylated PNP 14 was immuno‐precipitated from rat brain synaptosomes labeled metabolically with [32P]orthophosphate. Injection of [32P]orthophosphate into the third ventricle of rat brain resulted in incorporation of radioactive phosphate into PNP 14. We have also found that Ca2+, calmodulin‐dependent protein kinase II phosphorylates serine residue(s) of PNP 14 in vitro. The results suggest that PNP 14 may be important to neuronal cells, but not to glial cells, and that its physiological functions may be controlled by the phosphorylation reaction.