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UNIT 1 UNE CHEM 1005 Questions With Complete Solutions $12.99
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UNIT 1 UNE CHEM 1005 Questions With Complete Solutions
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  • Course
  • CHEM 1005
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  • University Of New England (UNE )

Hemoglobin binds oxygen with a greater affinity in the: correct answer: R state Hemoglobin bound to heme is termed a holoprotein. The heme or porphoryin ring is required for oxygen binding and it is termed a: correct answer: prosthetic group Alpha helices and beta sheets are primarily stabi...

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  • July 27, 2023
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  • 2022/2023
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  • unit 1 une chem 1005 questions with complete solut

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  • University of New England (UNE )
  • CHEM 1005
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UNIT 1 UNE CHEM 1005 Questions
With Complete Solutions
Hemoglobin binds oxygen with a greater affinity in the: correct
answer: R state

Hemoglobin bound to heme is termed a holoprotein. The heme
or porphoryin ring is required for oxygen binding and it is
termed a: correct answer: prosthetic group

Alpha helices and beta sheets are primarily stabilized by: correct
answer: H bonding

Ligases are a class of enzymes characterized by their ability to:
correct answer: synthesize bonds between carbon atoms and an
additional atom that is involved in the cleavage of a high energy
bond.

An enzyme inhibitor that increases the Km but does not change
the Vmax is classified as: correct answer: competitive inhibitor

Cleavage of fructose 1, 6 bisphosphate to dihydroxyacetone and
glyceraldehyde 3-phosphate is achieved by what class of
enzymes: correct answer: lyase

Enzymes reduce the activation energy for a reaction. All
enzymes do this by: correct answer: providing an active site
most complementary the transition state, Enzymes help to
reduce the activation energy of a reaction by stabilizing high

,energy intermediates. By have a flexible active site that is highly
complementary to the transition state of a substrate this is most
readily achieved.

The activity of an enzyme is increased when the enzyme is
phosphorylated on an exposed tyrosine residue. Phosphorylation
of this amino acid is classified as which of the following?
correct answer: covalent modification, Phosphorylation is a
covlanet modification to an enzyme that can increase or
decrease the activity of an enzyme.

Under low energy conditions, AMP will bind to
phosphofructokinase I and glycogen phosphorylase. This is an
example of which of the follow types of enzyme regulation?
correct answer: allosteric activation

Which of the following is an example of enzyme regulation
through covalent modification? correct answer: Phosphorylation
of muscle glycogen phosphorylase

Movement of ammonia from an amino acid to an alpha-keto
acid involves a family of enzymes best categorized as: correct
answer: Transferases

An alpha-helical arrangement of amino acids is considered to be
part of what level of protein structure? correct answer:
secondary structure of the protein

An example of enzyme activation by cleavage is best illustrated
by which of the following? correct answer: activation of
chymotrypsinogen to chymotrypsin

, Coenzymes are complex nonprotein molecules that participate in
catalysis by providing functional groups that form a covalent
intermediate between the enzyme and the substrate. Which of
the following is an example of a coenzyme that participates in
an activation-transfer reaction? correct answer: Thiamaine
pyrophosphate (TPP)

Motifs are common structural elements that retain a particular
function within the protien. Which of the following is an
example of a protein motif? correct answer: An arrangment of
β-strands connected by α - helicies (βαβαβ)

What is an allosteric activator? correct answer: a. binds and puts
active site in optimal configuration which
favors substrate binding, higher efficiency
b. noncovalent, so reversible
c. also dependent on enzyme concentration

What is an allosteric inhibitor? correct answer: a. binds to
enzyme and changes shape of active site so substrate cannot
bind and enzyme is turned off
b. binding through noncovalent interactions so are reversible
c. whether or not they bind to enzyme depends on concentration
d. the mechanism behind feedback inhibition

Competitive inhibitors? correct answer: Compete with substrate
for binding at enzyme's substrate recognition site. This increases
Km because it increases the concentration of substrate needed to
saturate the enzyme, but no change to Vmax.

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