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Exam (elaborations)

BIOC 384 EXAM 3 QUESTIONS AND ANSWERS 2025

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Which state of glycogen phosphorylase gives the enzyme its highest activity? - phosphorylated glycogen phosphorylase Observe the ribbon structure of pepsin. To do this, click the green-outlined box at the bottom of the player. Green x's will appear over your selection. Then go to the dropdown menu and on the "Display" line, click the "Toggle Ribbon for selection" icon. Then click the "Toggle CPK for selection" icon to remove the space-filling display. To remove the green x's, click "Clear Selection" on the "Misc" line of the dropdown menu. Determine the relative proportions of secondary and quaternary structure(s). What best describes these structures? - The major secondary structures are beta sheets, and there is no quaternary structure. The catalytic acitivity and/or conformational stability of this protein is likely dependent upon ____________ of peripheral amino acid side chains. These side chains are expected to have a ______________ value. - protonation low pKa Which of the following correctly describes the biochemistry of the amino acids at the termini of pepsin? - two nonpolar amino acids at the N-terminus and one polar amino acid at the C-terminus Competitive Inhibitor - Does not affect the vmax of the reaction Binds to the active site of an enzyme Higher concentrations of substrate can reduce the effect of the inhibitor. The y-axis intercept of the Lineweaver-Burk plot remains the same with or without this inhibitor. Uncompetitive Inhibitor - Does not bind to the free enzyme Increasing inhibitor concentration decreases both the vmax and the Km. Mixed Inhibitor - Does not bind to the active site of an enzyme, but can bind to the free enzyme or the enzyme-substrate complex

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2024/2025
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BIOCHEM 384


BIOC 384 EXAM 3 QUESTIONS AND
ANSWERS 2025
Which state of glycogen phosphorylase gives the enzyme its highest activity? -
phosphorylated glycogen phosphorylase


Observe the ribbon structure of pepsin. To do this, click the green-outlined box at the
bottom of the player. Green x's will appear over your selection. Then go to the dropdown
menu and on the "Display" line, click the "Toggle Ribbon for selection" icon. Then click
the "Toggle CPK for selection" icon to remove the space-filling display. To remove the
green x's, click "Clear Selection" on the "Misc" line of the dropdown menu.


Determine the relative proportions of secondary and quaternary structure(s). What best
describes these structures? - The major secondary structures are beta sheets, and there is
no quaternary structure.


The catalytic acitivity and/or conformational stability of this protein is likely dependent
upon ____________ of peripheral amino acid side chains. These side chains are expected
to have a ______________ value. - protonation


low pKa


Which of the following correctly describes the biochemistry of the amino acids at the
termini of pepsin? - two nonpolar amino acids at the N-terminus and one polar amino
acid at the C-terminus


Competitive Inhibitor - Does not affect the vmax of the reaction


Binds to the active site of an enzyme

BIOCHEM 384

,BIOCHEM 384




Higher concentrations of substrate can reduce the effect of the inhibitor.


The y-axis intercept of the Lineweaver-Burk plot remains the same with or without this
inhibitor.


Uncompetitive Inhibitor - Does not bind to the free enzyme


Increasing inhibitor concentration decreases both the vmax and the Km.


Mixed Inhibitor - Does not bind to the active site of an enzyme, but can bind to the free
enzyme or the enzyme-substrate complex


Kinase enzymes phosphorylate other proteins and enzymes. This is a common
mechanism of covalently modifying enzymes in order to control their catalytic efficiency.
Which of the following amino acids is not targeted for phosphorylation by kinases? -
leucine


Which of the following activates a zymogen?


Enterokinase, Trypsinogen, Chymotrypsinogen, Pepsinogen - Enterokinase


Choose the correct statements about the function and activity of arrestin. - PKA
phosphorylation also modifies GPCR, leading to arrestin binding to the receptor for
endosomal transport.


Arrestin facilitates protein transport, which prevents a receptor from reassociating with
the G protein complex.

BIOCHEM 384

,BIOCHEM 384




Tasting involves many different cell-signaling processes that ultimately generate nerve
signals transduced by membrane depolarization. Sweet tastes result in PIP2 hydrolysis,
while salty tastes allow sodium ions to directly alter the membrane potential. What can
you deduce about the signaling mechanisms for sweet and salty? - Sodium ions directly
enter the cells, indicating the signal is transduced by an ion channel.


Sweet utilizes the GPCR signaling pathway, activating phospholipase C.


You have a mystery hormone (agonist), and to test the nature of the agonist you add it to
a dish of cultured liver cells. Shortly afterward you observe an increase in protein kinase
activity. In a second experiment, you find the kinase is inhibited if you add an adenylate
cyclase inhibitor to the cells prior to adding your mystery agonist. Which kind of receptor
system is the agonist signaling through? - GPCR


Glucagon binding to the glucagon receptor inhibits which of the following processes? -
Glycogen synthesis


While glucagon (a peptide) and epinephrine (a tyrosine derivative) are very different
agonists, both signal through GPCR systems. Some of the components of the pathways
are unique, while other signaling components are shared between both systems. Place
each item in the appropriate category: glucagon and epinephrine shared, glucagon
independent, or epinephrine independent.


Shared:


Glucagon Independent:


Epinephrine Independent: - Shared:
Net accumulation of glucose
BIOCHEM 384

, BIOCHEM 384


Adenylate cyclase activation
Gsa activation
cAMP signaling pathways


Glucagon:
Peptide binding to GPCR receptor


Epinephrine:
Ligand binding to adrenergic receptor
Activation of phospholipase C
Gqa activation


When ATCase is in the __________ state it indicates that ____________ is bound, and
that ATCase is ______________ regulated. - T; CTP; down


Consider the reaction shown below


(A) Identify the kind of chemical catalysis


(B) Identify which of the amino acids can act as X in the reaction


Choose ONE correct answer for each (A and B). - Acid-Base catalysis


TYR




BIOCHEM 384

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