Use our stage plan builder for venues and managers to share plots with artists who either perform at your venue or who work with you. After you share the plot, the artist can then create their stage plot by adding musicians and equipment to the plan.
Free Stage Plots For Bands
The potential of nematophagous fungi to control the free-living stages of nematode parasites of sheep: Pasture plot study with the fungus Duddingtonia flagrans. Vet. Parasitol. The experiment was designed to test the ability of D. flagrans to reduce infective larval populations on pasture after passage through the gastrointestinal tract of sheep. Merino sheep were given chlamydospores by intra-ruminal infusion at a rate of 5 million chlamydospores/sheep/day and faeces collected from these sheep was deposited on pasture plots. Numbers of larvae recovered from faeces and pasture were both lower on plots from sheep dosed with fungus (P
OnSong is a powerful app with way more features that you will ever use. You can load in lyric and chord charts and do fun things like beam messages to your bandmates (provided they're using the app too), broadcast your lyrics to other devices and screens (good for sing-alongs and worship bands), and even control your stage lighting (although this is a paid add-on).
Dimensionless Kratky plots of the free and bound protein are very similar (Fig. 3i) and the associated Porod-Debye plots do not plateau, making it unclear whether binding has any influence on flexibility (Fig. 3j). The RgD entropy calculations suggest that both the free and bound proteins are very flexible in that their RgD entropy values place them in the third and fourth quartiles of proteins in the BIOISIS and SASBDB databases (Figs 3i and 2d,e). Moreover, the calculated entropy for the bound state is larger than the entropy of the free protein, suggesting that the bound protein is more flexible than the unbound protein. However, it should be noted that the difference between these values are quite small and within the range of error associated with RgD calculations (n.b. the errors associated with RgD calculations on C3b are 0.01, as shown in Supplementary Table S3). Since binding of Efb stabilizes the open state, these calculations suggest that the bound, and predominantly open, state is able to sample a range of radii of gyration that is similar to, or possibly larger than, that of the unbound protein.
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