1F23 Lab 1 Statistics Introduction
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In this activity, you will study the effect of temperature on lactase activity. By the end of this activity, you should be able to: a.
analyze data related to enzyme activity. b.
identify the components of the scientific method. c.
summarize your lab data. •
To gather the data for the lab activity, go to the following website: https://exchange.iseesystems.com/public/jon-darkow/lactase-enzyme-simulation-with-data-
analysis/index.html#page4 •
Open and run the Lactase Simulation website. Record your data and summarize your data. •
Submit a lab write up document on Canvas by 1159PM Sunday. Experiment I: The effect of temperature on lactase activity.
Click on the Simulate tab. The standard condition settings are lactose for 500 mg/dL, pH at 7.0 and temperature at 25
0
C, and 5 mmol lactase solution. You will vary one of these conditions in this experiment. In this experiment, you will be varying temperature. The condition you are varying is the independent variable for that experiment. The outcome you measure for that experiment is the dependent variable. The hypothesis of an experiment is a tentative proposed relationship of the independent and dependent variable of the experiment. I.
Identify the independent variable, dependent variable, and hypothesis of your experiment. II.
Set the simulation to standard initial lactose (500 mg/dL), pH (7.0), and lactase solution (5 mmol). Run 5 simulations at a temperature of ___
0
C. Record the glucose concentration (mg/dL) at 4, 7 and 11 minutes. Temperature _____
0
C 4 minutes 7 minutes 11 minutes Run 1 Run 2 Run 3 Run 4 Run 5 Mean Range Standard Deviation Using the above data to determine the mean, range, and standard deviation of your samples at 4, 7, and 11 minutes. Transfer the mean, range and standard deviation numbers to the Statistics Introduction Summary table.
III.
Set the simulation to standard initial lactose (500 mg/dL), pH (7.0), and lactase solution (5 mmol). Run 5 simulations at ___
0
C. Record the glucose concentration (mg/dL) at 4, 7 and 11 minutes. Temperature ______ C 4 minutes 7 minutes 11 minutes Run 1 Run 2 Run 3 Run 4 Run 5 Mean Range Standard Deviation Transfer the mean, range and standard deviation numbers to the Statistics Introduction Summary table. IV.
Set the simulation to standard initial lactose (500 mg/dL), pH (7.0), and lactase solution (5 mmol). Run 5 simulations at ___ C. Record the glucose concentration (mg/dL) at 4, 7 and 11 minutes. Temperature______
0
C 4 minutes 7 minutes 11 minutes Run 1 Run 2 Run 3 Run 4 Run 5 Mean Range Standard Deviation Transfer the mean, range and standard deviation numbers to the Statistics Introduction Summary table.
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Related Questions
Please handraw this graph with all the necessary detailed information:
Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
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Examine the graph showing the rate of reaction versus temperature for an enzyme–catalyzed reaction in a human.
a. Describe what is happening to the enzyme at around 40°C.
b. Explain why the line touches the x-axis at approximately 20°C and 45°C.
c. Average body temperature for humans is 37°C. Suggest a reason why the temperature optimum of this enzyme is greater than 37°C.
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Include some background information on amylase and enzyme activity. Include the hypotheses that are being testing in each of the three enzyme experiments. Predict the results of each of the three experiments based on your hypotheses (if/then). Analyze the results of the temperature, pH, and enzyme concentration experiments. Note the optimum temperature and pH if possible. Note environmental factors that restrict enzyme activity.
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Please complete the following question. There is no need to provide an explaination.
13
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What are the correct terms that go with the definition?
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Leia wants to determine the effect of enzyme concentration on enzyme activity using potato samples and hydrogen peroxide. However, her results do not follow the theoretical trend and thus she can't draw any conclusions from the data obtained. What might have caused errors in the experiment?
I. Placing potato samples under room temperature
II. Different treatments, with potato being proportional to the volume of hydrogen peroxide
III. Placed the same amount of hydrogen peroxide for a different amount of potatoes
IV. Placed the same amount of potatoes for a different volume of hydrogen peroxide
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Suppose in your biochemistry class you are given an enzyme and you are asked to determine whether egg or the starch is the
substrate for this enzyme. Arrange the following statements such that it explains how you would go about doing this task from first
step to the last step (you can drag and drop the choices to arrange from the first step to the last step):
Drag and drop options into correct order and submit. For keyboard navigation. SHOW MORE V
First take three test tubes labeled as A / B and C. A is the negative control and just add buffer. To the test-tube B add
5ml of raw egg in buffer. To tube C add 5 ml of starch solution in buffer
After 30 minutes of incubation - take the three tubes out and divide the content of each tube into to two tubes. So you
will now have total of 6 tubes - two for control - two 'B' tubes and two 'C' tubes
First you will test to determine if the substrate is egg : To one set of tubes A/B and Cadd ninhydrine - appearance of
= blue or brown or yellow…
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Please complete the following question.
13
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Which of the following statement on the process of enzyme production is false?
Select one:
a. Agglomeration is sometimes used to increase solubility of enzyme powder
b. After fermentation, intracellular enzymes can be directly extracted by filtration
c. Spray drying can be used to dry the enzyme products into powder forms
d. Chromatography is used to purify the enzyme produced
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Please choose one of these answers
A. An allosteric inhibitor appeared
B. There was a dramatic change jn the pH.
C. The enzyme had achieved its maximum velocity.
D. The enzyme had denatured
E. A large amount of the substrate had been consumed.
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The following statements are either True or False. Please label accordingly.
a.
L-Amino reductase is an enzyme.
b.
Allosteric enzymes are composed of two or more protein chains.
Heavy metals are examples of inhibitors.
They function by binding to sulfur on cysteine amino acid residues.
C.
d.
A reversible noncompetitive inhibitor temporarily blocks an enzyme's active site.
Enzymes don't denature as easily as smaller proteins when heated or
stressed due to their complex secondary and tertiary structure.
e.
Oxidative phosphorylation is the biochemical process by which ATP is
synthesized from ADP when protons cross the inner mitochondrial membrane.
f.
g.
DNA and RNA strands differ only in the fact that DNA forms a double helix.
h.
There is no secondary structure in RNA strands.
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The investigators examined the
behavior of the ATCase enzyme
in the presence of CTP, and in
the presence of both CTP and
ATP. The concentration of
CTP is 0.1 mM and the concen-
tration of ATP is 2 mM. The
results are shown in Figure
3. What is the significance of
these observations?
% Activity
100
90
80
70
60
50
40
30
20
10
0
control
+ CTP
+CTP +ATP
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Refer to image below and answer the following:
1. What is the optimum temperature (degrees celsius) for the enzyme activity?
2. At what temperature when the emzyme was totally denatured?
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Please make a diagram showing the process of how to make amylase. The diagram can be to the making of any protein, starting with the dna in the nucleus and ending with the exocytosis of the salivary amylase out of the cells in the salivary glands. Please show work and pictures. Thank you.
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Please answer as comprehensive as possible.
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The FMO3 enzyme has an important physiological function in people. State the normal substrate of FMO3 in people and describe a genetic polymorphism that can reduce the activity of this enzyme. Describe the consequence to people with the reduced FMO3 activity. Give at least one reference from the primary literature (i.e. a scientific journal) to support your answer.
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Which of the following is a primary function of the active site of an enzyme?
a.
It binds allosteric regulators of the enzyme.
b.
It binds noncompetitive inhibitors of the enzyme.
c.
It catalyzes the reaction associated with the enzyme.
d.
It is activated by the presence of the end product of the metabolic pathway in which the enzyme is involved.
Clear my choice
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Question text
Which of the following statement about the mass spectrometry is true?
a.
Large amount of protein sample is needed for mass spectrum, and thus it is very expensive.
b.
It is a powerful method to determine the 3-dimensional structure of proteins.
c.
It can be sued for protein location in a living cell.
d.
It can be used to measure the molecular weight of proteins.
e.
It can be used to determine the stability of a protein structure in solution.
Clear my choice…
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Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________1. Name: alkaline phosphataseReaction: a phosphate monoester + H2O = an alcohol + phosphate_____________________2. Reaction: L-threonine = D-threonine.Other information: Inverts both chiral centers, a racemase. _____________________3. Name: glycine-N-acylaseReaction: acyl-COA + glycine = CoA + N-acylglycine_____________________ 4. Name: lysine decarboxylaseReaction: L-lysine = cadaverine + CO2 _____________________5. Name: methanol dehydrogenaseReaction: methanol + NAD+ = formaldehyde + NADH + H+ _____________________6. Name: citryl-CoA synthetaseReaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA_____________________7. Name: D-xylulose reductaseReaction: xylitol + NAD+ = D-xylulose + NADH + H+ _____________________8. Name: cellobiose phosphorylaseReaction: cellobiose phosphate =…
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Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________1. Name: alkaline phosphataseReaction: a phosphate monoester + H2O = an alcohol + phosphate_____________________2. Reaction: L-threonine = D-threonine.Other information: Inverts both chiral centers, a racemase. _____________________3. Name: glycine-N-acylaseReaction: acyl-COA + glycine = CoA + N-acylglycine_____________________ 4. Name: lysine decarboxylaseReaction: L-lysine = cadaverine + CO2
_____________________5. Name: methanol dehydrogenaseReaction: methanol + NAD+ = formaldehyde + NADH + H+
_____________________6. Name: citryl-CoA synthetaseReaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA_____________________7. Name: D-xylulose reductaseReaction: xylitol + NAD+ = D-xylulose + NADH + H+
_____________________8. Name: cellobiose phosphorylaseReaction: cellobiose phosphate =…
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The catalytic activity of enzymes depends on the presence of appropriate environmental
conditions. Pepsin is a digestive enzyme found in the stomach and facilitates the digestion
of large proteins.
If pepsin is removed from this acidic environment of the stomach and is instead placed in
a more basic environment, it will cease to function. Describe the specific effect that a
change in environmental pH will have on pepsin and explain how this change can lead to
inhibition of its catalytic activity.
Respond in 4 to 6 complete sentences.
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Consider the following data set of enzymes A, B C and D which catalyze the same
reaction.
Enzyme A km = 5mM Vmax = 225MM/sec
Enzyme B km = 50mM Vmax = 430mM/sec
Enzyme C km = 15mM Vmax = 235mM/sec
%3D
Enzyme D km
12mM Vmax = 533mM/sec
When concentrations of substrate are very low, which is the enzyme that is
producing most product?
MacBook Air
DO
F5
S0
# 12
F4
F3
%
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Fill in the blanks and answer the question:
A. The enzyme ATCase (aspartate transcarbamoylase) uses _________________control to regulate its activity. The molecule ATP is an allosteric _____________ of ATCase and because it is a molecule different from the substrate of this enzyme it produces an _________________ effect in the enzyme’s activity.
B. Is it appropriate to study the enzymatic activity of ATCase with the Michaelis Menten approximation? Justify your answer.
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What are the biological actions of enzymes ? What reactions do they catalyze?
please include citation
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Describe and discuss which factors influence the choice of bioreactor design?(in long explanation please)
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Fill the box with the correct answers.
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Define the following terms:a. oxidoreductaseb. lyasec. ligased. transferasee. hydrolasef. isomerase
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Consider the reaction:
Galactose 1-phosphate + UDP-glucose → UDP-galactose + glucose 1-phosphate
Which pairing correctly matches the enzyme class and Enzyme Commission number for the
enzyme that catalyzes this reaction?
translocase; 2
translocase; 7
transferase; 2
transferase; 7
isomerase; 5
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Briefly explain the relationship between substrate concentration and enzyme activity and be sure to discuss situation in your answer
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What would be the control variables if any and the controls use in this experiment?
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A biologist investigating enzyme function plotted the activity of a particular enzyme (y-axis) vs pH (x-axis). Experiment A was performed at 30 oC, experiment B at 10 oC and experiment C at 100 oC. Experiments A, B, and C all used the same type of enzyme, they simple tested the enzyme's activity at different temperatures. Using your knowledge of enzyme activity, answer the questions based on the results shown in the graph. (Answer questions A) Graph included
A. Explain why A and B are so different.
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lace the description with the appropriate step in the enzymatic reaction.
The enzyme changes
shape, resulting in an
induced fit between
substrate and enzyme.
Glucose and galactose
are released, and the
enzyme is free to bind
other substrates.
Lactose
Galactose
Glucose-
Substrate: Lactose
Enzyme: Lactase
2
1
Enzyme-substrate complex
The bond is broken
between glucose and
galactose
3
The substrate, lactose,
binds to the enzyme
forming an enzyme-
substrate complex
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The purpose of this experiment is to determine how the activity of an enzyme can change under certain conditions: temperature, pH, substrate concentration
Introduction Purpose statement is specific, complete and uses proper scientific vocabulary Hypothesis statement is clear, logical and scientifically sound Contains sufficient background information relevant to the lab Accurate use of examples and scientific terminology Clear, concise (max 1 page; single spaced) Step 1: Obtain a sample amount of a hard fruit or vegetable, such as an apple, cut it into smaller equal pieces, and measure on a digital scale of 10g. Step 2: Get 100ml of room temperature tap water and add it into a glass cup, heat it on a hot plate until reaches 37 Celsius Step 3: Add the apple sample into the glass cup with the tap water and mix gently. Let the mixture to sit for 5 minutes. Step 4: With a kitchen thermometer measure the temperature of the apple mixture. Step 5: In a glass cup add 3mL of 3% hydrogen…
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Refer to the following graph when answering questions.
These words may be used to fill: competitive, uncompetitive, noncompetitive,
irreversible.
-1
mg
, μmol min-1
v-1
0.2
0.1
THA
-4-2
CBA
+
2 4
[S]-1, (mM-1)
Word
1, The value of Km for the enzyme depicted by curve A is
2, The value of Vmax for the enzyme depicted by curve A is
3, Curve B depicts the effect of an inhibitor on the system described by curve A.
This inhibitor is a
inhibitor.
4, Curve C depicts the effect of a different inhibitor of the system described by curve
A. This second inhibitor is a
inhibitor.
D
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- Please complete the following question. There is no need to provide an explaination. 13arrow_forwardWhat are the correct terms that go with the definition?arrow_forwardLeia wants to determine the effect of enzyme concentration on enzyme activity using potato samples and hydrogen peroxide. However, her results do not follow the theoretical trend and thus she can't draw any conclusions from the data obtained. What might have caused errors in the experiment? I. Placing potato samples under room temperature II. Different treatments, with potato being proportional to the volume of hydrogen peroxide III. Placed the same amount of hydrogen peroxide for a different amount of potatoes IV. Placed the same amount of potatoes for a different volume of hydrogen peroxidearrow_forward
- Suppose in your biochemistry class you are given an enzyme and you are asked to determine whether egg or the starch is the substrate for this enzyme. Arrange the following statements such that it explains how you would go about doing this task from first step to the last step (you can drag and drop the choices to arrange from the first step to the last step): Drag and drop options into correct order and submit. For keyboard navigation. SHOW MORE V First take three test tubes labeled as A / B and C. A is the negative control and just add buffer. To the test-tube B add 5ml of raw egg in buffer. To tube C add 5 ml of starch solution in buffer After 30 minutes of incubation - take the three tubes out and divide the content of each tube into to two tubes. So you will now have total of 6 tubes - two for control - two 'B' tubes and two 'C' tubes First you will test to determine if the substrate is egg : To one set of tubes A/B and Cadd ninhydrine - appearance of = blue or brown or yellow…arrow_forwardPlease complete the following question. 13arrow_forwardWhich of the following statement on the process of enzyme production is false? Select one: a. Agglomeration is sometimes used to increase solubility of enzyme powder b. After fermentation, intracellular enzymes can be directly extracted by filtration c. Spray drying can be used to dry the enzyme products into powder forms d. Chromatography is used to purify the enzyme producedarrow_forward
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