The proteins within the Tallaganda velvet worm slime have an expanded grip because their lack of secondary structure prevents them from binding to themselves.
Even though the s in the tallaganda velvet worm’s only make up 3-5% of the slime, the solid they create still binds the prey effectively. The proteins make the most of their presence because they can bind over a larger surface area due to their lack of secondary structure. Secondary structures, such as the alpha or beta sheet, are what cause a single protein to fold and take a 3-D shape. Without this structure, the tallaganda velvet worm proteins remain linear, so there is more room for neighboring protein strands to latch on and bind to each other. Essentially, it creates a larger available surface for bonds, which makes the resulting structure bind tighter and stronger than would normally be expected for that protein size.
This strategy was contributed by Rachel Major
