Although theoretically recognized for several decades as a common intermediate in many organic reactions, carbocations were unobservable because they were a short-lived, unstable class of compound.
14% of proteins fell into the unstable class, and 13% were assigned to the stable class.
This is supported by an under-representation of glycosylation modifications in the unstable class.
We found that signaling proteins were highly over-represented in the P1 unstable class (Fisher's exact test, P = 3.08e-29).
This resulted in 29% of proteins being assigned to an unstable class, and 26% to a stable class (Table 5).
There was also a smaller, though still significant over-representation of signaling proteins in the original unstable class determined by cluster analysis (Fisher's exact test, P = 0.019).
For P2, proteins scoring less than 0.3 were assigned to the unstable class and those scoring greater than 0.7 were assigned to the stable class.
Approximately 20% of the proteins fell into the unstable class, another 20% into the stable class, and the final 60% fell into the non-assigned class.
We used a subset of proteins contained in our "stable" class that overlapped with the "extra long" class used by [ 7], as well as a subset of our "unstable" class that overlapped with their "short" class.
The results from the statistical analyses on proteins in the unstable class are summarized in Table 2, and Table 3 contains the results for proteins assigned to the stable class.
We took a subset of proteins that overlapped with their "extra long" class and our stable class, as well as a subset of proteins that overlapped with their "short" class and our unstable class.
