📘 biochemistry

1. **Problem Statement:** We are given concentration values and corresponding absorbance (T1, T2, T3) readings. We need to find the IC50 value, which is the concentration at which

1. Problem 1: Given enzyme concentration $[E] = 1 \times 10^{-4}$ mM and substrate concentrations $[S]$ with initial velocities $V_o$, find $V_{max}$ and $K_M$ using the Lineweaver

1. Problem 2: Calculate the rate of reaction at substrate concentration $[S] = 3$ mM with and without the inhibitor. Given that no explicit kinetics constants are provided, assume

1. Enzyme activity variation with pH: Enzymes have an optimal pH at which their active site is most effective. Deviations from this pH can alter the enzyme's structure or the ioniz

1. **Problem statement:** Given enzyme kinetics data for amyloglucosidase with substrate concentration [S] and initial velocity $V_0$, determine $V_{max}$ and $K_M$ using the Linew

1. **Problem 1: Using the Lineweaver-Burk plot to find Vmax and KM** Given enzyme concentration = $1\times10^{-4}$ mM.

1. **Problem:** Calculate the rate of reaction at [S] = 3 mM with and without inhibitor for an oxidase enzyme with $V_{max} = 20$ μmol/min, $K_m = 2$ mM without inhibitor and appar

1. **Problem:** Calculate the rate of reaction at substrate concentration $[S]=3$ mM with and without inhibitor for an oxidase enzyme with $V_{max}=20$ $\mu$mol/min and $K_m=2$ mM