Answer:
Protein B has a higher affinity for ligand C than protein A
Explanation:
Binding affinity is a measure of the strength of the bonds or interactions between a single biomolecule or receptor to its ligand. A ligand is usually a small molecule that binds to a specific receptor.
The receptor is usually a large molecule that contains a specific site for the binding of ligand.
Binding affinity is usually measured by the equilibrium dissociation constant (KD). The equilibrium dissociation constant KD is a ratio of the dissociation and the association of ligand to the receptor. The value of KD is used to evaluate and compare the strengths of bimolecular interactions. The larger the KD value, the more weakly the target molecule and ligand are attracted to and bind to one another.
The higher the dissociation constant (KD), the weaker the affinity is between the interacting molecules, whereas, the smaller the KD value, the greater the binding affinity of the ligand for its target.
Protein B has a KD value of 10⁻⁹ M while Protein A has a KD of 10⁻⁶ M.
Ration of KD of protein B to protein A = 10⁻⁹ M/10⁻⁶ M = 10⁻³
Therefore, protein B has a KD value which is 1000 times smaller than the KD of protein A.
Weather satellites help show where the warm fronts and cold fronts are plus weather what counts are in the air! This helps them know it’s it’s going to rain snow or be sunny
Here is the correct answer: <span>Most homologous pairs look alike. They carry genes for the same characteristics and line up on the chromosome in the same order
i hope this helps you out</span>
Prokaryotic cells are simpler than eukaryotic cells. This is because prokaryotic cells have a single circular chromosome, no nucleus, and few other organelles. Eukaryotic cells have many chromosomes inside a nucleus, and they also have more organelles.
Answer:
Oxygen is being released through the Stomata
Option (A)
