An experimental investigation of edge strain and bow in roll forming a V-section

V-sections were roll formed from two grades of steel, and the strain on the top and bottom of the strip near the edge was measured using electrical resistance strain gauges. The channels were bent to a radius of 2 and 15 mm along the centerline. The steel strips were of mild and dual phase steel of yield strength 367 MPa and 597 MPa respectively. The longitudinal bow was measured using a 3-dimensional scanning system. The strain measurements were analysed to determine bending and mid-surface strains at the edge during forming. The peak longitudinal edge strain increased with material yield strength for both profile radii. For the 15 mm radius, the bow was larger in the dual phase steel than in the mild steel. For the 2 mm profile radius, the bow was smaller compared with the 15 mm profile radius and it was similar for both steels. It was observed that the difference between the peak longitudinal edge strain and yield strength to Youngs modulus ratio of the material is an important factor in determining longitudinal bow.

Potassium channel modulation by a toxin domain in matrix metalloprotease

Peptide toxins found in a wide array of venoms block K+ channels, causing profound physiological and pathological effects. Here we describe the first functional K+ channel-blocking toxin domain in a mammalian protein. MMP23 (matrix metalloprotease 23) contains a domain (MMP23TxD) that is evolutionarily related to peptide toxins from sea anemones. MMP23TxD shows close structural similarity to the sea anemone toxins BgK and ShK. Moreover, this domain blocks K+ channels in the nanomolar to low micromolar range (Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4, in decreasing order of potency) while sparing other K+ channels (Kv1.2, Kv1.5, Kv1.7, and KCa3.1). Full-length MMP23 suppresses K+ channels by co-localizing with and trapping MMP23TxD-sensitive channels in the ER. Our results provide clues to the structure and function of the vast family of proteins that contain domains related to sea anemone toxins. Evolutionary pressure to maintain a channel-modulatory function may contribute to the conservation of this domain throughout the plant and animal kingdoms.

Queensland northern quolls are not immune to cane toad toxin

The release of the highly toxic South American cane toad (Bufo marinus) to the toad-free Australian continent in 1935, and their subsequent rapid spread over large areas of tropical Australia, has resulted in a massive decline of predators such as yellow-spotted goannas (Varanus panoptes) and northern quolls (Dasyurus hallucatus). In spite of dramatic declines of northern quoll populations in the Northern Territory, a few populations still persist in areas of Queensland where northern quolls have co-existed with toads for several decades

Isolation breeds naivety : island living robs Australian varanid lizards of toad-toxin immunity via four-base-pair mutation

Since their introduction to the toad-free Australian continent cane toads (Bufo marinus) have caused a dramatic increase in naïve varanid mortality when these large lizards attempt to feed on this toxic amphibian. In contrast Asian–African varanids, which have coevolved with toads, are resistant to toad toxin. Toad toxins, such as Bufalin target the H1-H2 domain of the α1 subunit of the sodium-potassium-ATPase enzyme. Sequencing of this domain revealed identical nucleotide sequences in four Asian as well as in three African varanids, and identical sequences in all 11 Australian varanids. However, compared to the Asian–African varanids, the Australian varanids showed four-base-pair substitutions, resulting in the alteration in three of the 12 amino acids representing the H1-H2 domain. The phenotypic effect of the substitutions was investigated in human embryonic kidney (HEK) 293 cells stably transfected with the Australian and the Asian–African H1-H2 domains. The transfections resulted in an approximate 3000-fold reduction in resistance to Bufalin in the Australian HEK293 cells compared to the Asian–African HEK293 cells, demonstrating the critical role of this minor mutation in providing Bufalin resistance. Our study hence presents a clear link between genotype and phenotype, a critical step in understanding the evolution of phenotypic diversity.