Final answer:
The rapid degradation of cyclin would decrease the activity of the Cdk, leading to decreased phosphorylation of target proteins and consequently, more cells being detained at the cell cycle checkpoints.
Step-by-step explanation:
An environmental change that leads to the degradation of cyclin at a faster rate would generally have the effect of decreasing the activity of cyclin-dependent kinases (Cdks). This is because cyclins must be bound to Cdks to form a fully active complex which then phosphorylates other proteins, thereby advancing the cell through the checkpoints of the cell cycle. With the degradation of cyclins at a higher rate, there would be a decreased phosphorylation of the target proteins. This decrease would mean that more cells will be stopped at the checkpoint, as the cell cycle cannot progress without proper phosphorylation signals. Therefore, the correct answer to the question is:
The accelerated degradation of cyclin would tend to decrease the activity of the Cdk, lead to decreased phosphorylation of the target protein, and result in more cells being stopped at the checkpoint.
As a result, there would be decreased phosphorylation of the target protein. The Cdk/cyclin complex phosphorylates the target protein to activate it and move the cell cycle forward. However, with decreased Cdk activity, there would be fewer phosphorylation events.
This would ultimately lead to more cells being stopped at the checkpoint. The target protein plays a role in advancing the cell cycle, so its decreased phosphorylation would hinder cell cycle progression, resulting in more cells being halted at the checkpoint.