61. In a cell, a repressor binds to its cognate operator with a KD = 10-9M. The cellular concentration of the
repressor is 10-8M. The extent of repressor bound to the operator is:
1. 100%
2. 50%
3. 37%
4. 0%
Calculating Repressor Binding to Operator: A KD-Based Approach
In gene regulation, repressors play a crucial role by binding to operator sequences to prevent transcription. The strength of this binding is characterized by the dissociation constant (KD) — a critical value in understanding protein-DNA interactions.
What Is KD?
KD (dissociation constant) is the concentration of the repressor at which 50% of the operator sites are occupied. It reflects the affinity between a repressor and its binding site:
-
A lower KD means stronger binding affinity.
-
A higher KD implies weaker binding.
The Binding Equation
The fraction of operator bound by the repressor at a given concentration [L][L] is calculated as:
Fraction bound=[L][L]+KD\text{Fraction bound} = \frac{[L]}{[L] + K_D}
Where:
-
[L][L] = concentration of the repressor
-
KDK_D = dissociation constant
Given in the Question:
-
KD=10−9 MK_D = 10^{-9} \, \text{M}
-
[L]=10−8 M[L] = 10^{-8} \, \text{M}
Substitute into the equation:
Fraction bound=10−810−8+10−9=10−81.1×10−8≈0.91\text{Fraction bound} = \frac{10^{-8}}{10^{-8} + 10^{-9}} = \frac{10^{-8}}{1.1 \times 10^{-8}} \approx 0.91
This means approximately 91% of the operator sites are occupied by the repressor.
Closest Matching Option:
None of the options says 91%, but 100% is the closest approximation, indicating nearly complete binding due to high repressor concentration compared to KD.
Final Answer:
1. 100%
This is a reasonable approximation based on the math, where the repressor concentration is much higher than KD, resulting in nearly complete occupancy of operator sites.