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chapter 5 lehninger biochemistry 2024-2025
when oxygen binds to a heme-containing protein, the two open coordination bonds of fe2+ are
occupied by:
a) one o atom and one amino acid atom.
b) one o2 molecule and one amino acid atom.
c) one o2 molecule and one heme atom.
d) two o atoms.
e) two o2 molecules. - answer-b
in the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the
fraction of binding sites occupied can best be described as:
a) hyperbolic.
b) linear with a negative slope.
c) linear with a positive slope.
d) random.
e) sigmoidal. - answer-a
the interactions of ligands with proteins:
a) are relatively nonspecific.
b) are relatively rare in biological systems.
c) are usually irreversible.
d) are usually transient.
e) usually result in the inactivation of the proteins. - answer-d
a prosthetic group of a protein is a non-protein structure that is:
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a) a ligand of the protein.
b) a part of the secondary structure of the protein.
c) a substrate of the protein.
d) permanently associated with the protein.
e) transiently bound to the protein. - answer-d
which of the following statements about protein-ligand binding is correct?
a) the ka is equal to the concentration of ligand when all of the binding sites are occupied.
b) the ka is independent of such conditions as salt concentration and ph.
c) the larger the ka (association constant), the weaker the affinity.
d) the larger the ka, the faster is the binding.
e) the larger the ka, the smaller the kd (dissociation constant). - answer-e
myoglobin and the subunits of hemoglobin have:
a) no obvious structural relationship.
b) very different primary and tertiary structures.
c) very similar primary and tertiary structures.
d) very similar primary structures, but different tertiary structures.
e) very similar tertiary structures, but different primary structures. - answer-e
an allosteric interaction between a ligand and a protein is one in which:
a) binding of a molecule to a binding site affects binding of additional molecules to the same site.
b) binding of a molecule to a binding site affects binding properties of another site on the protein.
c) binding of the ligand to the protein is covalent.
chapter 5 lehninger biochemistry 2024-2025
when oxygen binds to a heme-containing protein, the two open coordination bonds of fe2+ are
occupied by:
a) one o atom and one amino acid atom.
b) one o2 molecule and one amino acid atom.
c) one o2 molecule and one heme atom.
d) two o atoms.
e) two o2 molecules. - answer-b
in the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the
fraction of binding sites occupied can best be described as:
a) hyperbolic.
b) linear with a negative slope.
c) linear with a positive slope.
d) random.
e) sigmoidal. - answer-a
the interactions of ligands with proteins:
a) are relatively nonspecific.
b) are relatively rare in biological systems.
c) are usually irreversible.
d) are usually transient.
e) usually result in the inactivation of the proteins. - answer-d
a prosthetic group of a protein is a non-protein structure that is:
, Page 2 of 6
a) a ligand of the protein.
b) a part of the secondary structure of the protein.
c) a substrate of the protein.
d) permanently associated with the protein.
e) transiently bound to the protein. - answer-d
which of the following statements about protein-ligand binding is correct?
a) the ka is equal to the concentration of ligand when all of the binding sites are occupied.
b) the ka is independent of such conditions as salt concentration and ph.
c) the larger the ka (association constant), the weaker the affinity.
d) the larger the ka, the faster is the binding.
e) the larger the ka, the smaller the kd (dissociation constant). - answer-e
myoglobin and the subunits of hemoglobin have:
a) no obvious structural relationship.
b) very different primary and tertiary structures.
c) very similar primary and tertiary structures.
d) very similar primary structures, but different tertiary structures.
e) very similar tertiary structures, but different primary structures. - answer-e
an allosteric interaction between a ligand and a protein is one in which:
a) binding of a molecule to a binding site affects binding of additional molecules to the same site.
b) binding of a molecule to a binding site affects binding properties of another site on the protein.
c) binding of the ligand to the protein is covalent.
