When the gene mutates, however, the resulting protein collapses on itself and can clog the blood vessels.
Fluorescence resonance energy transfer (FRET) is one of the few methods available to measure the rate at which a folding protein collapses.
The ET data show that, under solvent conditions favoring the folded protein, collapsed non-native structures are not substantially more stable than extended conformations, and that the two populations interchange rapidly.
That the higher mass KCNE2 protein collapsed into the lower size with sample heating suggests that it represented a dimer of the 20kDa form (Figure 5B).
As discussed below, the purified protein collapses to a single band following chymotrypsin treatment to remove the propeptides, i.e., these mobility differences do not reflect differences within the triple helical collagen structure.
Our observations validate the force-clamp technique as a powerful approach to determining the free-energy landscape of proteins collapsing and folding from extended states.
During the release period, the protein can collapse to a manifold of compact states or refold.
Left too long, however, and the protein structure collapses into an unpalatable, stinky mess.
Fluid accumulation interferes with gas exchange, and can cause the alveoli to fill with proteins and collapse due to edema and bleeding.
