Assessing the road-damaging potential of heavy vehicles

The relative influence of various heavy vehicle design features on road-damaging potential is discussed. Testing procedures that could be used to measure the road-damaging potential of heavy vehicles are examined. A validated vehicle simulation is used to examine some of the characteristics of dynamic tyre forces generated by typical leaf sprung and air sprung articulated heavy vehicles for typical highway conditions. The proposed EC suspension test is simulated and the results compared with dynamic tyre forces generated under highway conditions. It is concluded that the road-damaging potential of a vehicle cannot be assessed by the simplistic parametric measurement of the proposed EC test. It is questionable whether a vehicle that passes the test will be any more 'road friendly' than one that fails.

THEORETICAL ROAD DAMAGE DUE TO DYNAMIC TYRE FORCES OF HEAVY VEHICLES. PART 1: DYNAMIC ANALYSIS OF VEHICLES AND ROAD SURFACES.

Theory is presented for simulating the dynamic wheel forces generated by heavy road vehicles and the resulting dynamic response of road surfaces to these loads. Sample calculations are provided and the vehicle simulation is validated with data from full-scale tests. The methods are used in the accompanying paper to simulate the road damage done by a tandem-axle vehicle.

THEORETICAL ROAD DAMAGE DUE TO DYNAMIC TYRE FORCES OF HEAVY VEHICLES. PART 2: SIMULATED DAMAGE CAUSED BY A TANDEM-AXLE VEHICLE.

The literature relating to road surface failure and design is briefly reviewed and the conventional methods for assessing the road damaging effects of dynamic tire forces are examined. A new time domain technique for analyzing dynamic tire forces and four associated road damage criteria are presented. The force criteria are used to examine the road damaging characteristics of a simple tandem-axle vehicle model for a range of speed and road roughness conditions. It is concluded that for the proposed criteria, the theoretical service life of road surfaces that are prone to fatigue failure may be reduced significantly by the dynamic component of wheel forces. The damage done to approximately five per cent of the road surface area during the passage of a theoretical model vehicle at typical highway speeds may be increased by as much as four times.

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 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.