`No dream is ever just a dream': Stanley Kubrick's Eyes Wide Shut as monofilm

This article examines Stanley Kubrick's final film, Eyes Wide Shut (1999), in relation to its source text, J.M.Q. Davies's 1999 translation of Arthur Schnitzler's Traumnovelle/Dream Story, originally published in 1926. Both the film and the novel are viewed through the lens of monodrama, a dramatic genre characterized by the attempt to convey the subjective psychical experience of a strong central protagonist. Monodramatic traits may also be found in the novel and film, and the article explores how this adaptation typifies certain aspects of the monodrama form and how those traits are portrayed through the specific conventions and limitations of the differing media.

Determining propeller induced erosion alongside quay walls in harbours using Artificial Neural Networks

In shallow waters, such as those found close to berth structures, the wash from a manoeuvring ship’s propeller can cause erosion of the seabed. This erosion can be increased if the wash intersects a berth structure. A number of researchers have undertaken model studies and used regression analysis to develop predictive relationships for the scouring action. This paper presents an experimental investigation with Artificial Neural Networks (ANN’s), used to analyse the results. The purpose of using ANN’s was to examine the prediction accuracy of the Networks in comparison with previous regression analysis methods. ANN’s were found to provide a more accurate method of predicting propeller wash scour than the equations presented by previous investigators.

Interfacial self-assembly of a bacterial hydrophobin

The majority of bacteria in the natural environment live within the confines of a biofilm. The Gram-positive bacterium Bacillus subtilis forms biofilms that exhibit a characteristic wrinkled morphology and a highly hydrophobic surface. A critical component in generating these properties is the protein BslA, which forms a coat across the surface of the sessile community. We recently reported the structure of BslA, and noted the presence of a large surface-exposed hydrophobic patch. Such surface patches are also observed in the class of surface-active proteins known as hydrophobins, and are thought to mediate their interfacial activity. However, although functionally related to the hydrophobins, BslA shares no sequence nor structural similarity, and here we show that the mechanism of action is also distinct. Specifically, our results suggest that the amino acids making up the large, surface-exposed hydrophobic cap in the crystal structure are shielded in aqueous solution by adopting a random coil conformation, enabling the protein to be soluble and monomeric. At an interface, these cap residues refold, inserting the hydrophobic side chains into the air or oil phase and forming a three-stranded β-sheet. This form then self-assembles into a well-ordered 2D rectangular lattice that stabilizes the interface. By replacing a hydrophobic leucine in the center of the cap with a positively charged lysine, we changed the energetics of adsorption and disrupted the formation of the 2D lattice. This limited structural metamorphosis represents a previously unidentified environmentally responsive mechanism for interfacial stabilization by proteins.