Influence of ground anchors on topographic amplification at slope crests

One feature of earthquake loading in regions containing sloping ground is a marked increase in accelerations at the crests of slopes. Many field cases exist where such increased accelerations were measured. The observed increase in the amount and severity of observed building damage near the edge of cliff-type topographies has been attributed to the topographic amplification. To counter this, it has been shown that anchoring the soil mass responsible for this to the rest of the stable soil mass can reduce the amount of topographic amplification. In this study, dynamic centrifuge modelling will be used to identify the region affected by topographic amplification in a model slope. The soil accelerations recorded will be compared to those measured in a comparable model treated by anchors. In addition, the tension measured in the anchors will be examined in order to better understand how the anchors are transferring the loads and mitigating these amplifications. © 2010 Taylor & Francis Group, London.

Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.

Ure2p is the protein determinant of the Saccharomyces cerevisiae prion state [URE3]. Constitutive overexpression of the HSP70 family member SSA1 cures cells of [URE3]. Here, we show that Ssa1p increases the lag time of Ure2p fibril formation in vitro in the presence or absence of nucleotide. The presence of the HSP40 co-chaperone Ydj1p has an additive effect on the inhibition of Ure2p fibril formation, whereas the Ydj1p H34Q mutant shows reduced inhibition alone and in combination with Ssa1p. In order to investigate the structural basis of these effects, we constructed and tested an Ssa1p mutant lacking the ATPase domain, as well as a series of C-terminal truncation mutants. The results indicate that Ssa1p can bind to Ure2p and delay fibril formation even in the absence of the ATPase domain, but interaction of Ure2p with the substrate-binding domain is strongly influenced by the C-terminal lid region. Dynamic light scattering, quartz crystal microbalance assays, pull-down assays and kinetic analysis indicate that Ssa1p interacts with both native Ure2p and fibril seeds, and reduces the rate of Ure2p fibril elongation in a concentration-dependent manner. These results provide new insights into the structural and mechanistic basis for inhibition of Ure2p fibril formation by Ssa1p and Ydj1p.

Influence of tire geometry on the horn effect

A reciprocal-configuration Boundary Element Method calculation of acoustic radiation characteristics has been implemented for a generic tire geometry. The influence of the geometric parameters on the radiation characteristics has been studied. The degree of amplification of noise sources on the tire belt is strongly affected by the overall tire width. In contrast, the tire radius predominantly influences the pattern of the varying amplification around the belt, rather than its absolute level. Radiusing the tire's 'shoulder' region is potentially beneficial in terms of lowering amplification levels, for a tire of fixed overall width. However, it is less effective than maintaining sharp shoulders and reducing the overall width. Thus, for an acoustically optimal belted tire, the overall width should be as small as possible, even if this leads to a larger diameter. The width should not be increased in order to accommodate a radiused crown region. Copyright © (2012) by the Institute of Noise Control Engineering (INCE).

Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2.

Ure2p is the protein determinant of the Saccharomyces cerevisiae prion state [URE3]. Constitutive overexpression of the HSP70 family member SSA1 cures cells of [URE3]. Here, we show that Ssa1p increases the lag time of Ure2p fibril formation in vitro in the presence or absence of nucleotide. The presence of the HSP40 co-chaperone Ydj1p has an additive effect on the inhibition of Ure2p fibril formation, whereas the Ydj1p H34Q mutant shows reduced inhibition alone and in combination with Ssa1p. In order to investigate the structural basis of these effects, we constructed and tested an Ssa1p mutant lacking the ATPase domain, as well as a series of C-terminal truncation mutants. The results indicate that Ssa1p can bind to Ure2p and delay fibril formation even in the absence of the ATPase domain, but interaction of Ure2p with the substrate-binding domain is strongly influenced by the C-terminal lid region. Dynamic light scattering, quartz crystal microbalance assays, pull-down assays and kinetic analysis indicate that Ssa1p interacts with both native Ure2p and fibril seeds, and reduces the rate of Ure2p fibril elongation in a concentration-dependent manner. These results provide new insights into the structural and mechanistic basis for inhibition of Ure2p fibril formation by Ssa1p and Ydj1p.