Crystal-Field Paschen-Back Effect on Ruby in Ultrahigh Magnetic Fields

Zeeman spectra of the R lines of ruby (Cr$^{3+}$: $\alpha$-Al$_{2}$O$_{3}$) were studied in ultrahigh magnetic fields up to 230 T by magneto-photoluminescence measurements. The observed Zeeman patterns exhibit nonlinear behaviors above 100 T, evidencing the breakdown of the previously reported Paschen-Back effect for ${\bf B} \perp c$ geometry. We adopted the crystal-field multiplet theory including the cubic crystal field (${\mathcal H}_{\rm cubic}$), the trigonal crystal field (${\mathcal H}_{\rm trig}$), the spin-orbit interaction (${\mathcal H}_{\rm SO}$), and the Zeeman interaction (${\mathcal H}_{\rm Z}$). It is found that the nonlinear splitting of the R lines is owing to the hybridization between the $^{2}E$ and $^{2}T_{1}$ states, which leads to the quantization of these Zeeman levels with the orbital angular momentum. Our results suggest that the exquisite energy balance among ${\mathcal H}_{\rm cubic}$, ${\mathcal H}_{\rm trig}$, ${\mathcal H}_{\rm SO}$, and ${\mathcal H}_{\rm Z}$ realized in ruby offers a unique opportunity to observe the onset of the $crystal-field$ Paschen-Back effect toward the high-field extreme.Comment: 8 pages, 7 figure

Liquid and solid oxygen under ultrahigh magnetic fields

学位の種別: 課程博士審査委員会委員 : （主査）東京大学准教授 松田 康弘, 東京大学教授 有馬 孝尚, 東京大学教授 嶽山 正二郎, 東京大学教授 岩佐 義宏, 東京大学教授 竹谷 純一University of Tokyo(東京大学

Magnetostriction studies up to megagauss fields using fiber Bragg grating technique

We here report magnetostriction measurements under pulsed megagauss fields using a high-speed 100 MHz strain monitoring system devised using fiber Bragg grating (FBG) technique with optical filter method. The optical filter method is a detection scheme of the strain of FBG, where the changing Bragg wavelength of the FBG reflection is converted to the intensity of reflected light to enable the 100 MHz measurement. In order to show the usefulness and reliability of the method, we report the measurements for solid oxygen, spin-controlled crystal, and volborthite, a deformed Kagom\'{e} quantum spin lattice, using static magnetic fields up to 7 T and non-destructive millisecond pulse magnets up to 50 T. Then, we show the application of the method for the magnetostriction measurements of CaV$_{4}$O$_{9}$, a two-dimensional antiferromagnet with spin-halves, and LaCoO$_{3}$, an anomalous spin-crossover oxide, in the megagauss fields.Comment: 9pages, 6 figures, Conference proceedings for MegaGauss16 at Kashiwa, Japan in Sept. 201

Isolation of a Drosophila gene coding for a protein containing a novel phosphatidylserine-binding motif

金沢大学医薬保健研究域薬学系To elucidate the molecular basis of the binding of proteins to the membrane phospholipid phosphatidylserine (PS), we characterized PS-binding peptides isolated from a phage display library. Amino acid sequences deduced from the nucleotide sequences of over 60 phage clones isolated revealed that there was no common primary structure among these peptides, but all peptides were rich in basic amino acid residues. In particular, 15 clones encoded peptides that contained contiguous arginine residues. Characterization of two such peptides in more detail showed that they bound to PS, and to a much lower extent to other phospholipids, including phosphatidylinositol, phosphatidylethanolamine, and phosphatidylcholine. Unlike other Ca2+-dependent PS-binding proteins, these peptides did not require Ca2+ for binding to PS, and the addition of Ca2+ did not alter the phospholipid specificity. Substitution of one of the two RR sequences in one peptide by alanine had no effect, but that of both sequences completely abolished the activity. Furthermore, we identified a Drosophila gene coding for a presumed nuclear protein that shares an amino acid sequence, including a RR residue, with one of the two PS-binding peptides. This protein bound to PS partly depending on the presence of the RR residue. These results allowed us to conclude that an amino acid sequence including contiguous arginine residues is a novel motif that defines Ca2+-independent PS-binding activity. © 2005 The Japanese Biochemical Society