An allosteric interaction between a ligand and a protein is one in which: multip

Question

An allosteric interaction between a ligand and a protein is one in which: multiple molecules of the same ligand can bind to the same binding site. Binding of the ligand to the protein is covalent. Two different ligands can bind to the same binding site. Binding of a molecules to a binding site affects binding properties of another site on the protein. Binding of a molecules to a binding site affects binding additional molecules to the same site. In an alpha helix, the R groups on the amino acid residues: alternate between the outside and the inside of the helix. Cause only right handed helices to form. Are found on the outside of the helix spiral. Stack within the interior of the helix. Generate the hydrogen bonds that form the helix. Amino acids are ampholytes they can function as either an: neutral molecule of an ion. Polar or a nonpolar molecule. Standard or a nonstandard monomer in proteins transparent or a light-absorbing compound. Acid or a base. Starch and glycogen are both polymers of glucose 1 phosphate sucrose fructose D glucose D glucose.

Explanation / Answer

[41] An allosteric interaction between ligand and protein is one in which,

d. bonding of a molecule to a binding sites affects binding properties on another site on the protein.

[42] In an alpha-helix, the R group of amino acid residues,

c. are found on the outside of the helix spiral

[43] amino acids are ampholytes because they can function as either a(n):

e. acid or a base

[44] Starch and glycogen are both polymers of,

d. alpha-D-glucose

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