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.
Answer:
parent cell diploid cells
Explanation:
Yes the orchard grass is a consumer. it consumes water and sunlight
Answer:
sarcomeres
Explanation: A contracting skeletal muscle fiber typically shortens as all of its sarcomeres do this.... Thick and thin protein filaments in sarcomeres interact to cause.... True or false, thick and thin filaments maintain their same length whether the muscle is relaxed or contracted?
<span>The frontal and parietal bones of the skull are susceptible to compressed skull fractures. This is especially important in newborn babies. There is a location in the skull called the Anterior Fontanelle, where two frontal and 2 parietal bones meet. This area of the skull is very soft until as late as 2 years old.</span>
