the answer is a.
i say this is the answer because whenever you’re doing a scientific hypothesis you’re mostly observing and making assumptions.
<span>They often move much greater distances than the intact protein.</span>
The nucleotide variation is obtained by comparing nucleotide sequence between individuals between individuals of a particular population. If genetic variability is 0 % then the number of alleles would be 1.
<h3>
What is genetic variability?</h3>
Genetic variability is the evolutionary process and development of new species. Genetic variability describes the dissimilarities such as brown eyes, blue eyes that happen naturally when DNA is altered.
Genetic variability varies in population. Genetic variability describes the tendency at which traits in a population may vary.
Gene variation refers to a differences in the genetic makeup of the individual. Genetic variation is a important process of natural selection and biological evolution.
Therefore, The nucleotide variation is obtained by comparing nucleotide sequence between individuals between individuals of a particular population. If genetic variability is 0 % then the number of alleles would be 1.
To learn more about genetic variation, refer to the link :
brainly.com/question/848479
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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.
