Partial soi power LDMOS with a variable low-kappa; Dielectric buried layer and a buried P layer

A power LDMOS on partial silicon on insulator (PSOI) with a variable low-κ dielectric (VLKD) buried layer and a buried p (BP) layer is proposed (VLKD BPSOI). At a low κ value, the electric field strength in the buried dielectric (EI) is enhanced, and a Si window makes the substrate share the vertical voltage drop, leading to a high vertical breakdown voltage (BV). Moreover, three interface field peaks are introduced by the BP, the Si window, and the VLKD, which modulate the fields in the SOI layer, the VLKD layer, and the substrate; consequently, a high BV is obtained. Furthermore, the BP reduces the specific on-resistance (Ron), and the Si window alleviates the self-heating effect (SHE). The BV for VLKD BPSOI is enhanced by 34.5%, and Ron is decreased by 26.6%, compared with those for the conventional PSOI, and VLKD BPSOI also maintains a low SHE. © 2006 IEEE.

Role of f electrons in the Fermi surface of the heavy fermion superconductor beta-YbAlB4.

We present a detailed quantum oscillation study of the Fermi surface of the recently discovered Yb-based heavy fermion superconductor beta-YbAlB4. We compare the data, obtained at fields from 10 to 45 T, to band structure calculations performed using the local density approximation. Analysis of the data suggests that f holes participate in the Fermi surface up to the highest magnetic fields studied. We comment on the significance of these findings for the unconventional superconducting properties of this material.

Measurement of the Interaction Between Recombinant I-domain from Integrin alpha 2 beta 1 and a Triple Helical Collagen Peptide with the GFOGER Binding Motif Using Molecular Force Spectroscopy.

The role of the collagen-platelet interaction is of crucial importance to the haemostatic response during both injury and pathogenesis of the blood vessel wall. Of particular interest is the high affinity interaction of the platelet transmembrane receptor, alpha 2 beta 1, responsible for firm attachment of platelets to collagen at and around injury sites. We employ single molecule force spectroscopy (SMFS) using the atomic force microscope (AFM) to study the interaction of the I-domain from integrin alpha 2 beta 1 with a synthetic collagen related triple-helical peptide containing the high-affinity integrin-binding GFOGER motif, and a control peptide lacking this sequence, referred to as GPP. By utilising synthetic peptides in this manner we are able to study at the molecular level subtleties that would otherwise be lost when considering cell-to-collagen matrix interactions using ensemble techniques. We demonstrate for the first time the complexity of this interaction as illustrated by the complex multi-peaked force spectra and confirm specificity using control blocking experiments. In addition we observe specific interaction of the GPP peptide sequence with the I-domain. We propose a model to explain these observations.