1 × 4 space switching and simultaneous all-optical wavelength conversion at 2.488Gbit/s using a single monolithically integrated multiwavelength laser

A novel InGaAs/InGaAsP/InP integrated multiwavelength grating cavity laser is presented, which has been used to demonstrate space switching and simultaneous all-optical wavelength conversion at bit rates of 2.488 Gbit/s. This has been achieved using a single monolithically integrated device without the need for post-filtering to separate the converted signal from the input.

1.4 kV, 25 A, PT and NPT Trench IGBTs with optimum forward characteristics

In this paper we report the development of 1.4 kV 25 A PT and NPT Trench IGBTs with ultra-low on-resistance, latch-up free operation and highly superior overall performance when compared to previously reported DMOS IGBTs in the same class. We have fabricated both PT and transparent anode NPT devices to cover a wide range of applications which require very low on-state losses or very fast time with ultra-low switching losses. The minimum forward voltage drop at the standard current density of 100A/cm2 was 1.1 V for PT non-irradiated devices and 2.1 V for 16 MRad PT irradiated devices. The non-irradiated transparent emitter NPT structure has a typical forward voltage drop of 2.2 V, a turn-off time below 100 ns and turn-off energy losses of 11.2 mW/cm2 at 125 C. The maximum controllable current density was in excess of 1000A/cm2.

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.