A8 Assignment worksheet - How genes shape the niche DrP(1)
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1. Find and list the amino acid positions that show some differences between
the three (3) species? (2.5pts)
2. For this part, use the table below to list the amino acid positions where both
warm-adapted species have changed compared to the cold-adapted species, and also what those amino acid changes were. (2.5pts)
Position
Number
From
Cold-Adapted Amino
Acid
To
Warm-Adapted Amino
Acid
220
D ASPARTATE
E GLUTAMATE
225
K LYSINE
N ASPARAGINE
310
E GLUTAMATE
D ASPARTATE
219
T THREONINE
A ALANINE
3. Of the amino acid changes identified in part 2, use the table below to list (a) ONLY those changes which also result in a change in the chemical properties
of the amino acid R-groups (e.g. polar vs. nonpolar) and (b) what those property changes were. (You may not need all rows). (2.5pts)
Position
Number
From
Cold-Adapted R-
Group Property
To
Warm-Adapted R-
Group Property
225
Electrically charged
(polar) K
Polar side-chains
219
Polar T
Non-polar A
4. Assuming that these amino acid changes are adaptations to warm temperatures in the warm-adapted species, how would these changes be expected to affect the flexibility (or rigidity) of the protein/enzyme?
(2.5pts)
Allows these species to be able to swim faster in the warmer waters, since less polarity in their side chains signify less interaction with the water molecules (hydrophobia/less hydrogen bonds)
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b. Д5,11,14
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5. The following Figure for Question 5 shows a simplified Nitrogen Cycle driven
entirely by microorganisms.
(i) :
(ii) :
(iii) :
(iv) :
N₂
(V) :
N₂O
iv
NO
NH3
NO₂
(a) Name the five major nitrogen transformation processes numbered (i) to (v) in the
simplified Nitrogen Cycle.
ii
iii
NO₂
The figure for Question 5
Organic Nitrogen
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1. Refer to Model 2 for information relevant to this question
a) A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values?
b) What is the pI of Lys-Glu-Ser?
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13. Draw the structure of the amino acid lysine showing the correct protonation states of its acid and base
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14. Draw the structure of the amino acid lysine showing the correct protonation states of its acid and base
functional groups in a solution of lysine at pH 8.5. What is the net overall charge on lys at this
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pH?
"Draw the structure of the amino acid Histidine showing the correct protonation states of its acid and base
functional groups in a solution of his at pH 5. What is the net overall charge on his at this pH?" etc...)
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6. Amino acid alanine containing N5 isotope in a-amino group was administrated
to mouse with food. It was found that the N5 has rapidly appeared in a-amino
groups of aspartate, glutamate and other amino acids in the liver (with the
exception of lysine and threonine). Explain, why does it occur? For the answer:
412
Chapter 8. Nitrogen metabolism
a) draw the reactions of aspartate and glutamate formation with alanine
participation;
b) describe enzymes catalyzing these types of reactions; specify coenzyme;
c) specify the group of amino acids due to the possibility that they have been
synthesized in the body and Glu, Ala, and Asp relate to.
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11. Refer to the figure below.
нн
Н
`NH2
NH2
N'
N-
2e-+H*
R
NAD+
NADH
NAD+ functions as a coenzyme in many enzyme-catalyzed reactions. The changes that take place in this coenzyme are the same for all of these reactions and are illustrated in the figure. It is
likely that, in these reactions, NAD+
functions as an electron acceptor (reducing agent) in redox reactions.
functions as an electron donor (oxidizing agent) in redox reactions.
functions as a base in acid-base catalytic mechanisms.
functions as an electron donor (oxidizing agent) in redox reactions.
functions as an electron acceptor (oxidizing agent) in redox reactions.
+Z-
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1
of
on 12
ed
dout of
ag
on
man
The nitrogen cycle involves the movement of atmospheric nitrogen
through a series of nitrifying bacteria, which process the nitrogen
into forms that can be absorbed and used by other living organisms,
Which of the following paths best represent the correct order of this
process, starting with atmospheric nitrogen and ending with a form
of nitrogen that most plants (producers) can use?
Select one:
O a. N2(g) → ammonium → nitrite → nitrate
-
b. nitrite →→ ammonium →→ N2(g) →→ nitrate
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c. nitrate → N2(g) → ammonium → nitrate
d. ammonium nitrate → nitrite → N2(g)
Complete the table below using the dropdown choices.
Human
Activity
Expand
city
suburbs
Large
cattle
ranches
Replant
forested
areas
Effect on cellular functions
MacBook
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der these chemical species by increasing pH of an 0.1 M aqueous solution of each. That is, imagine making an 0.1 M solution of each species. Select 1 next
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Notice that some of the rankings have been filled in for you already. Also notice that water is on the list. For that particular case, just compare the pH of pure
water to the pH of the other solutions.
Note for advanced students: for all charged species, you may assume the necessary counterions act as neither acids nor bases.
species
relative pH of
0.1 M aqueous solution
☑
ك
+
C6H5NH3
2
CH3NH2
(Choose one)
CIO2
(Choose one)
CH,NH,
(Choose one)
OH
CH3NH3
H₂O
+
8 (highest)
3
(Choose one)
HCIO2
1 (lowest)
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sentences)
Pair #1
Ketogenic, glucogenic or both
Prevalence in peptides and proteins
Role in biosynthesis
Role in homeostasis (e.g. ammonia)
Aspartic acid
Glutamic acid
Important in which pathways
Pair #2
Arginine
Histidine
Ketogenic, glucogenic or both
Prevalence in peptides and proteins
Role in biosynthesis
Role in homeostasis (e.g. ammonia)
Pair #3
Ketogenic, glucogenic or both
Prevalence in peptides and proteins
Role in biosynthesis
Role in homeostasis (e.g. ammonia)
Important in which pathways
Tyrosine
Phenylalanine
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O B. E. coli don't have protein disulfide isomerase in their ER
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O D. E. coli don't have a Golgi
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-Inhibitor
+Inhibitor
[S] (mM).
V&νβσπ:(μmol/sec)
V0&νβσπ&ν βσπ;(μmol/sec)
0.0001
33
17
0.0005
71
50
0.001
83
67
0.005
96
91
0.01
98
95
What is the Vmax of this enzyme WITHOUT iinhibitor?
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D) Aand B
E) All of the Above
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3. Aspartate aminotransferase (AspAT) catalyzes the following reaction:
COO™
C=O
CH₂
COO
Oxaloacetate
The AspAT enzyme has two active-site arginines, Arg 386 and Arg 292, that interact with the a-
carboxylate and ß-carboxylate groups on the aspartate substrate, respectively. Investigators stud-
ied the mechanism of AspAT in more detail by constructing mutant AspAT enzymes in which
either or both of the essential arginines were replaced with a lysine residue. The kinetic parame-
ters for the wild-type enzyme and nutant enzymes are shown in the table.
NH—CH-COO
T
CH₂
COO™
Aspartate
α-Amino acid
Enzyme
1. Wild-type Asp AT(Arg 292 Arg 386)
2. Mutant Asp AT(Lys 292 Arg 386)
3. Mutant Asp AT(Arg 292 Lys 386)
4. Mutant Asp AT(Lys 292 Lys 386)
Asp-AT
a-Keto acid
KM (MM)
4
326
72
300
Kcat (S-1)
530
4.5
9.6
0.055
(a)
The Michaelis constant is strictly not equivalent to an equilibrium binding constant;
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-Inhibitor
+Inhibitor
[S] (mM)
V0&νβσπ;(μmol/sec).
νο&νβσπ: &ν βσπ (μmol/sec)
0.0001
33
17
0.0005
71
50
0.001
83
67
0.005
96
91
0.01
98
95
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47.
Which of the following is true under the following conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 mM. (1 nM = 10-9 M, 1 μM=10-6 M, 1 mM = 10-3 M)
Group of answer choices
Between 0% and 50% of active sites have substrate bound
0% of active sites have substrate bound
50% of active sites have substrate bound
100% of active sites have substrate bound
Between 50% and 100% of active sites have substrate bound
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UTSASE (the arrow indicates the peptide bond cleaved in each case).
Substrate
Km(mM)
kcat(s)
PAPALG
4.0
26
РАPАLA
1.5
37
РАРАLF
0.64
18
Based on the above data shown for UTSAse what features of amino acid sequence dictate the specificity of
the proteolytic cleavage?
A. Large hydrophilic R-groups
B. Large hydrophobic R-groups
C. Neutral R-groups
D. Small hydrophilic R-groups
E. Large hydrophobic R-groups
F. Negatively charged R-groups
G. Positively charged R-groups
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