Formation of silicon-on-insulator layers by electron beam recrystallization

This paper outlines the development of the electron beam recrystallization approach to the formation of silicon-on-insulator layers. The technique of recrystallizing seeded layers by a line electron beam has been widely adopted. Present practice in electron beam recrystallization is reviewed, both from materials and process points of view. Applications of silicon-on-insulator substrates formed in this way are described, particularly in three-dimensional integration. © 1988.

An experimental and computational study of the formation of a streamwise shed vortex in a turbine stage

Shear layers shed by aircraft wings roll up into vortices. A similar, though far less common, phenomenon can occur in the wake of a turbomachine blade. This paper presents experimental data from a new single stage turbine that has been commissioned at the Whittle Laboratory. Two low aspect ratio stators have been tested with the same rotor row. Surface flow visualisation illustrates the extremely strong secondary flows present in both NGV designs. These secondary flows lead to conventional passage vortices but also to an intense vortex sheet which is shed from the trailing edge of the blades. Pneumatic probe traverse show how this sheet rolls up into a concentrated vortex in the second stator design, but not in the first. A simple numerical experiment is used to model the shear layer instability and the effects of trailing edge shape and exit yaw angle distribution are investigated. It is found that the latter has a strong influence on shear layer rollup: inhibiting the formation of a vortex downstream of NGV 1 but encouraging it behind NGV 2.

Probing small molecule binding to amyloid fibrils.

Much effort has focussed in recent years on probing the interactions of small molecules with amyloid fibrils and other protein aggregates. Understanding and control of such interactions are important for the development of diagnostic and therapeutic strategies in situations where protein aggregation is associated with disease. In this perspective article we give an overview over the toolbox of biophysical methods for the study of such amyloid-small molecule interactions. We discuss in detail two recently developed techniques within this framework: linear dichroism, a promising extension of the more traditional spectroscopic techniques, and biosensing methods, where surface-bound amyloid fibrils are exposed to solutions of small molecules. Both techniques rely on the measurement of physical properties that are very directly linked to the binding of small molecules to amyloid aggregates and therefore provide an attractive route to probe these important interactions.

Satellite formation in drop-on-demand printing of polymer solutions

High speed photographic images of jets formed from dilute solutions of polystyrene in diethyl phthalate ejected from a piezoelectric drop-on-demand inkjet head have been analyzed in order to study the formation and distribution of drops as the ligament collapses. Particular attention has been paid to satellite drops, and their relative separation and sizes. The effect of polymer concentration was investigated. The distribution of nearest-neighbour centre spacing between the drops formed from the ligament is better described by a 2-parameter modified gamma distribution than by a Gaussian distribution. There are (at least) two different populations of satellite size relative to the main drop size formed at normal jetting velocities, with ratios of about three between the diameters of the main drop and the successive satellite sizes. The distribution of the differences in drop size between neighbouring drops is close to Gaussian, with a small non-zero mean for low polymer concentrations, which is associated with the conical shape of the ligament prior to its collapse and the formation of satellites. Higher polymer concentrations result in slower jets for the same driving impulse, and also a tendency to form ligaments with a near-constant width. Under these conditions the mean of the distribution of differences in nearest-neighbour drop size was zero.

The morphology of decorated amyloid fibers is controlled by the conformation and position of the displayed protein.

Self-assembled structures capable of mediating electron transfer are an attractive scientific and technological goal. Therefore, systematic variants of SH3-Cytochrome b(562) fusion proteins were designed to make amyloid fibers displaying heme-b(562) electron transfer complexes. TEM and AFM data show that fiber morphology responds systematically to placement of b(562) within the fusion proteins. UV-vis spectroscopy shows that, for the fusion proteins under test, only half the fiber-borne b(562) binds heme with high affinity. Cofactor binding also improves the AFM imaging properties and changes the fiber morphology through changes in cytochrome conformation. Systematic observations and measurements of fiber geometry suggest that longitudinal registry of subfilaments within the fiber, mediated by the interaction and conformation of the displayed proteins and their interaction with surfaces, gives rise to the observed morphologies, including defects and kinks. Of most interest is the role of small molecule modulation of fiber structure and mechanical stability. A minimum complexity model is proposed to capture and explain the fiber morphology in the light of these results. Understanding the complex interplay between these factors will enable a fiber design that supports longitudinal electron transfer.