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Trypsin cleaving a hypothetical protein at sites of phosphorylation, liberating a series of C-terminally phosphorylated peptides (see Knight et al. p 1047). The image was provided by Zachhary Knight at University of California, San Francisco and was made using the graphics program InsightII, rendering the crystal structure of trypsin as a ribbon underneath a transparent Connelly surface. The substrate is rendered as ball and stick, the phosphate groups in red. Artwork rendered by Erin Boyle.
Recent setbacks in product development at PPL Therapeutics illustrate the economic challenges and regulatory uncertainties that face protein production in GM animals.
Most life science investors have historically shied away from supporting agbiotechnology, but changing consumer acceptance and refinements in infrastructure, intellectual property management and regulations may make the sector more attractive in the coming years.
Characterization and manipulation of a novel prenyltransferase from monocot plant seeds reveal its capacity to produce tocotrienols and increase this form of vitamin E in transgenic plants by 10- to 15-fold.