UNE Biochemistry Midterm| 140 Questions|
With Complete Solutions
How do most enzymes reduce the activation energy needed to
move a reaction forward? correct answer: Providing an active
site most complementary the transition state
An enzyme has a mutation within the substrate binding of the
coenzyme needed for covalent catalysis. Which of the following
is likely to result as a consequence of this mutation? correct
answer: The enzyme will not be able to form the transition state
complex
Hemoglobin has the ability to display cooperative binding while
myoglobin does not display this binding kinetic pattern. Which
of the following differences between the two proteins accounts
for this difference in binding kinetics? correct answer: The
presence of quaternary structure in hemoglobin
Cleavage of fructose 1,6-bisphosphate to dihydroxy and
glyceraldehyde 3-phosphate is achieved by what class of
enzymes? correct answer: Lyase
Domains are common structural elements that retain a particular
function within the protein. Which of the following is an
example of a protein domain? correct answer: An arrangement
of beta strands connected to alpha helices (BaBaB)
,Covalent catalysis is used by many enzymes to cleave peptide
bonds. Which of the following amino acids would not facilitate
this type of catalysis? correct answer: Valine
Which of the following proteins is likely to have quaternary
structure? correct answer: A multimeric protein that contains
multiple peptide chains
What of the following best describes a protein domain? correct
answer: A relatively large pattern a three-dimensional structure
that is recognized across many proteins
Movement of ammonia from an amino acid to an a-keto acid
involved a family of enzymes best categorized as which of the
following? correct answer: Tranferases
A 19-year-old boy is diagnosed with Creutzfeldt-Jakob Disease
which is caused by the introduction of an amyloid fold in the
disease-causing protein. The introduction of this fold causes the
protein to transition from a primarily a-helix structure to an
aggregate of mostly B-sheets. This change in protein structure
(leading to disease) is best attributed to changes in which of the
following? correct answer: Folding of the secondary structures
Chymotropsin is a protease that cleaves peptide bonds. It is
characterized as which of the following classes of enzymes?
correct answer: Hydrolases
Which of the following best describes tertiary structure? correct
answer: Interactions between single amino acids adjacent to one
another
, Hemoglobin has the ability to display cooperative binding while
myoglobin does not display this binding pattern. Which of the
following differences between the two proteins accounts for the
difference in binding kinetics? correct answer: The presence of
quaternary structure in hemoglobin
Changes in the physiological variables listed below can alter the
affinity of hemoglobin for oxygen. Which of the following will
lower the affinity of hemoglobin for oxygen? correct answer:
Increase in 2,3 bisphosphoglycerate (BPG)
An enzyme has a mutation within the substrate binding site that
reduces the binding of the coenzyme needed for covalent
catalysis. Which of the following is likely to result as a
consequence of this mutation? correct answer: The enzyme will
not be able to form the transition state complex
An enzyme is participating in a general acid-base catalysis
reaction with an optimal reaction pH of 6.0. If acid is added to
the environment reducing the pH to 3, what is the likely impact
to the rate of reaction? correct answer: The rate of the reaction
is likely to decrease as the pH is out of optimal catalytic range
Which of the following best describes an enzyme inhibitor that
increases the Km but does not change the Vmax? correct
answer: A competitive inhibitor
The association of DNA and histones can be modified by
histone acetylation. A decrease in histone acetylation will have
With Complete Solutions
How do most enzymes reduce the activation energy needed to
move a reaction forward? correct answer: Providing an active
site most complementary the transition state
An enzyme has a mutation within the substrate binding of the
coenzyme needed for covalent catalysis. Which of the following
is likely to result as a consequence of this mutation? correct
answer: The enzyme will not be able to form the transition state
complex
Hemoglobin has the ability to display cooperative binding while
myoglobin does not display this binding kinetic pattern. Which
of the following differences between the two proteins accounts
for this difference in binding kinetics? correct answer: The
presence of quaternary structure in hemoglobin
Cleavage of fructose 1,6-bisphosphate to dihydroxy and
glyceraldehyde 3-phosphate is achieved by what class of
enzymes? correct answer: Lyase
Domains are common structural elements that retain a particular
function within the protein. Which of the following is an
example of a protein domain? correct answer: An arrangement
of beta strands connected to alpha helices (BaBaB)
,Covalent catalysis is used by many enzymes to cleave peptide
bonds. Which of the following amino acids would not facilitate
this type of catalysis? correct answer: Valine
Which of the following proteins is likely to have quaternary
structure? correct answer: A multimeric protein that contains
multiple peptide chains
What of the following best describes a protein domain? correct
answer: A relatively large pattern a three-dimensional structure
that is recognized across many proteins
Movement of ammonia from an amino acid to an a-keto acid
involved a family of enzymes best categorized as which of the
following? correct answer: Tranferases
A 19-year-old boy is diagnosed with Creutzfeldt-Jakob Disease
which is caused by the introduction of an amyloid fold in the
disease-causing protein. The introduction of this fold causes the
protein to transition from a primarily a-helix structure to an
aggregate of mostly B-sheets. This change in protein structure
(leading to disease) is best attributed to changes in which of the
following? correct answer: Folding of the secondary structures
Chymotropsin is a protease that cleaves peptide bonds. It is
characterized as which of the following classes of enzymes?
correct answer: Hydrolases
Which of the following best describes tertiary structure? correct
answer: Interactions between single amino acids adjacent to one
another
, Hemoglobin has the ability to display cooperative binding while
myoglobin does not display this binding pattern. Which of the
following differences between the two proteins accounts for the
difference in binding kinetics? correct answer: The presence of
quaternary structure in hemoglobin
Changes in the physiological variables listed below can alter the
affinity of hemoglobin for oxygen. Which of the following will
lower the affinity of hemoglobin for oxygen? correct answer:
Increase in 2,3 bisphosphoglycerate (BPG)
An enzyme has a mutation within the substrate binding site that
reduces the binding of the coenzyme needed for covalent
catalysis. Which of the following is likely to result as a
consequence of this mutation? correct answer: The enzyme will
not be able to form the transition state complex
An enzyme is participating in a general acid-base catalysis
reaction with an optimal reaction pH of 6.0. If acid is added to
the environment reducing the pH to 3, what is the likely impact
to the rate of reaction? correct answer: The rate of the reaction
is likely to decrease as the pH is out of optimal catalytic range
Which of the following best describes an enzyme inhibitor that
increases the Km but does not change the Vmax? correct
answer: A competitive inhibitor
The association of DNA and histones can be modified by
histone acetylation. A decrease in histone acetylation will have
