Sample result
One explained concept question
Why does a competitive inhibitor raise Km but leave Vmax unchanged?
Step by step
- A competitive inhibitor binds the active site, so it competes with the substrate.
- More substrate is needed to reach half of the maximum rate, so the apparent Km increases.
- At very high substrate concentrations the substrate outcompetes the inhibitor, so the enzyme can still reach the same Vmax.
- On a Lineweaver–Burk plot the lines cross at the y-axis: same 1/Vmax, different −1/Km.
A twelve-week outline
| Weeks | Focus |
|---|---|
| 1–4 | Biochemistry and biology content; one CARS passage a day |
| 5–7 | General and organic chemistry, physics; spaced review of weeks 1–4 |
| 8–9 | Psychology and sociology; first full-length practice test |
| 10–12 | A full-length every week with a full review day after each; light review in the final days |