BIOL201 Lab W03 Biological Macromolecules and BSA Standard Curve
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BIOL 201
Week 3: How do the components of biological molecules lead to their properties?
Lab: Biological Molecules
Completing and revising this activity should improve your proficiency with the following Learning Outcomes:
1.
EO4
Relate roles of biological molecules to the relevant chemical properties of those molecules
2.
EO4.1
Explain the properties of biological molecules using chemical principles.
3.
EO4.2
Describe the relevant properties of the biomacromolecules.
EO4.3
Compare the four biomacromolecules based on their chemical composition, chemical properties, and general functions.
Part 1. SUPP Research Project – Day 2
On Day 2 of the SUPP Research Project Protocol, we will be creating extracts for testing. This is similar
to the process that biomedical and biotech researchers utilize in drug discovery.
1.
Collect your team’s foil packages of dried material from Day 1 and grind the material into a fine powder.
2.
Transfer 1 g of dry, ground material to a labeled 1.5mL microcentrifuge tube and add 1mL methanol.
3.
Cap the tube tightly and vortex for 1 minute, steep for 15 minutes, vortex for 15 seconds, steep for a final 15 minutes.
4.
Centrifuge the microcentrifuge tubes at maximum speed for 1 minute. Be careful not to shake up the tube when you remove it from the centrifuge and while you are collecting the supernatant.
5.
Carefully collect the supernatant (liquid portion) into a new, labeled 1.5mL microcentrifuge tube. This is the sample extract.
6.
Save the extracts for next week’s experiment as instructed.
7.
Use the space below to:
a.
Record any interesting observations from this process.
b.
Make note of codes or abbreviations you used for your sample extract labels.
Part 2. Review of biomacromolecules
Living organisms are composed of chemical elements—mostly carbon, oxygen, nitrogen, and hydrogen (together accounting for 95% of mass) along with smaller amounts of other elements. Atoms of these elements combine to form molecules. There are four main classes of large molecules (macromolecules) in living things—proteins, nucleic acids, carbohydrates, and lipids. All these classes of large molecule 1
BIOL 201 Week 3 Lab -
are organic
molecules, meaning they are based on a carbon skeleton to which various “functional groups
” are attached. These functional groups include:
Amino
Carbonyl
Carboxyl
Hydroxyl
Sulfhydryl
Phosphate
R—NH
2
R—C—R
||
O
Ketone
R—C—H
||
O
Aldehyde
R—C—OH
||
O
R—OH
R—SH
O
||
R—O—P—O
-
|
O
-
Note the 2 extra electrons shown by the negative charges on the oxygens.
The “R” represents the rest of the molecule.
These functional groups are parts of small stable molecules (sugars, amino acids, nucleotides) which combine (polymerize) to make large complex molecules (polymers) such as carbohydrates, proteins, and DNA. Part 3. Identifying biomacromolecules
Caution: Some of the chemicals used in lab can injure skin and eyes. Please use extreme care with these chemicals and rinse with lots of water if you accidentally contact them.
Testing for the presence of starch in solutions
Iodine (I
2
) dissolved in potassium iodide (KI) solution interacts with starch, a coiled polymer of glucose, and turns dark blue-black from its original yellow-brown color. So, a positive reaction is dark blue-black,
and a negative reaction is a yellow-brown. It does not react with other carbohydrates that are not coiled.
Therefore, this is a positive test for the presence of starch.
Before you begin this test, predict
the outcome of the test for each tube.
To perform an Iodine Test for starch: 1.
Add 1 ml of each test solution to the appropriate test tube.
2.
Add three drops of the I
2
KI solution to each tube.
3.
Mix gently by swirling and record the results.
Iodine test for starch
Tub
e #
Test solution
Predict
-/+
Actual
-/+
Describe what you observed.
1
Distilled water
2
Potato blended in water
3
5% sucrose solution
4
1% starch solution
2
BIOL 201 Week 3 Lab -
List negative and positive control(s)
Testing for the presence of proteins in solutions: Coomassie Blue Test (also known as the Bradford Assay) for Protein
Proteins
are large polymers of amino acids. The amino acids are joined by peptide bonds (a peptide is a short chain of amino acids), in which the amino group of one amino acid is joined to the hydroxyl part of the acid (carboxyl) group on another, with the loss of a water molecule. There are 20 common kinds of amino acid in living organisms, with differing functional groups (denoted R below) on the other portions of the molecule.
Coomassie Brilliant Blue G-250 binds to specific amino acids, including basic and aromatic amino acids. Dye binding to amino acids causes the color of the solution to change from brown to blue. So, a positive reaction is blue and a negative reaction is brown. Again, before you begin this test, predict
the outcome of the test for each tube.
To perform a Coomassie Blue Test for protein: 1.
Add 2 ml of each test solution to the appropriate test tube.
2.
Add 1 ml of the Coomassie Blue reagent to each tube.
3.
Mix gently by capping the tube with a piece of parafilm & inverting, then record the results.
Protein test using Coomassie Blue reagent.
Tube
#
Test Solution
Predict
-/+
Actual
-/+
Describe what you observed.
1
Distilled water
2
Whole milk
3
Potato blended in water
a.
Which solutions are the positive control(s) and which are the negative control(s)?
You’ve now identified substances that contain starch and/or protein, but how much starch or protein is in each solution?
For Part 4 of this activity, you will creating a standard curve to use as a tool to determine the concentration of protein in an unknown solution. 3
BIOL 201 Week 3 Lab -
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Related Questions
las 2 act 3 and guide question
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Course Code: BIO-121
Chapter 3: Molecules of Life
Course Name: Principles Of Biology-1
5.
State the differences between starch and glycogen.
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Exercise B: Peptide Bond Formation
Figure 2 shows two individual amino acids, and then those same two amino acids after
they have been linked together by a peptide bond to form a dipeptide. Addition of
more amino acids linked by peptide bonds would form a polypeptide, the precursor to a
functional protein.
нн
+| | ||
H-N-C-Ĉ-0
H.
+! | ||
H-N-C-ċ –0
H.
H
H
H
+| | ||
H-N-C-C-N-C-C-
+
H
CH2
CH2
H
CH2
H.
CH2
SH
SH
NH,
NH,
Figure 2. Formation of a peptide bond between two amino acids.
Answer the below questions in your own document.
1. Which two amino acids are shown on the left side of Figure 2? Use the Figure
3.2 from your text to answer this.
2. To which chemical groups do these amino acids belong?
3. Were you able to identify their chemical characteristics based on your rules? If
not, you should go back and revise your rules!
On the dipeptide shown in Figure 2, label the peptide bond that was formed when the
two individual amino acids were joined. Label the free amino and carboxyl…
arrow_forward
Exercise B: Peptide Bond Formation
Figure 2 shows two individual amino acids, and then those same two amino acids after
they have been linked together by a peptide bond to form a dipeptide. Addition of
more amino acids linked by peptide bonds would form a polypeptide, the precursor to a
functional protein.
H
H
H.
H
H
+| |
H-N-Ċ- ċ-0
H-N-Ć- Ĉ-O
H-N-Č -C.
N-C-C-
H
CH2
H.
CH2
H.
CH2
H
CH2
SH
SH
NH2
NH2
Figure 2. Formation of a peptide bond between two amino acids.
Answer the below questions in your own document.
F1. Which two amino acids are shown on the left side of Figure 2? Use the Figure
They 3.2 from your text to answer this.
2. To which chemical groups do these amino acids belong?
3. Were you able to identify their chemical characteristics based on your rules? If
not, you should go back and revise your rules!
On the dipeptide shown in Figure 2, label the peptide bond that was formed when the
two individual amino acids were joined. Label the free amino and carboxyl groups at
the ends…
arrow_forward
Exercise B: Peptide Bond Formation
Figure 3 shows two individual amino acids, and then those same two amino acids after
they have been linked together by a peptide bond to form a dipeptide. Addition of
more amino acids linked by peptide bonds would form a polypeptide, the precursor to a
functional protein.
нн
H
H O
нно
H O
+| | ||
H-N-C-ċ-o +
+| 1 ||
H-N-C-C
+| | ||
Н-N—С- С—N—C—С
H
CH2
H
CH2
H
CH2
CH2
SH
SH
NH2
NH2
Figure 3. Formation of a peptide bond between two amino acids.
Answer the below questions in your own document.
• Which two amino acids are shown on the left side of Figure 3? Use Figure 2 to
answer this.
• To which chemical groups do these amino acids belong?
Were you able to identify their chemical characteristics based on your rules? If
not, you should go back and revise your rules!
On the dipeptide shown in Figure 3, label the peptide bond that was formed when the
two individual amino acids were joined. Label the free amino and carboxyl groups at
the ends of this…
arrow_forward
Need help on questions 3, 4, and 5.
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Learning Objectives
Identify a peptide bond, the N-terminus (amino-terminus) and C- terminus (carboxyl-terminus) of a polypeptide in a series of linked amino acids.
Describe the four levels of protein structure (primary, secondary, tertiary, and quaternary), what types of bonding interactions hold each level together, and how a protein’s structure relates to its cellular function.
Link the chemical structures of amino acid R groups to the types of interactions they could form in the folded structure of a protein.
Hypothesize the likely consequence of environmental conditions on the folded structure.
Recognize secondary structure elements when proteins are represented in different ways (e.g. ball-and-stick structures, ribbon diagrams).
Define these terms: enzyme, enzyme activity, active site, substrate, enzyme substrate complex, product, denature.
Explain with molecular detail how some conditions affect enzyme activity.
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ACTIVITY 12 - LIPIDS
As you watch the video, take notes about what you are learning about lipids. Images
have been provided to help you think about the information you are hearing.
Triglycerides are made from a glycerol and 3
fatty acids.
shutterst
beck
Phospholipids are important in the structure
of cells.
Cholesterol is used many ways in the body.
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B14U
A Goals
n Skills
Minds On
Actio
O Connect 2
Choose any two words in the table below, then connect them with a complete idea. Repeat this process three
times in total.
monomer
disaccharide
glucose
cell wall
energy
structure
glycosidic bond
isomer
cell-to-cell communication
For example: if the two words are ribosome and protein, then you could write: Ribosomes are connected to
proteins because the ribosomes are the protein builders in the cell. Ribosomes are made of two parts or
subunits. The larger of the 2 parts is where the ribosome can add on an amino acid to the growing protein
chain.
Practice good Organization skills by reviewing concepts and vocabulary from the whole Activity to include full
details.
Choose your best idea and share it with your classmates.
Join The Discussion
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BIOCHEMISTRY please help
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Please help with these quickly.
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Biomolecules Pre-Assessment
One similarity between carbohydrates and lipids is they both...
O contain nitrogen as part of their structure.
O are composed of fatty acid chains.
are made up of chains of smaller subunits.
act as enzymes and contain peptide bonds.
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Public Se x
S Schoology
O Microsoft Office Home
S Morrison's Speech: Your Page Pre x
ictims.seattleschools.org/common-assessment-delivery/start/5439383371?action=onresume&submissionld-682855653
Cellular Respiration and Digestion HW Quiz
POSSIBLE POINTS: 1.67
Polymers have
energy. After being broken down into monomers, the monomers have
energy
:: chemical
:: kinetic
: thermal
:: light
1
2
4
6.
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Plz help
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Need a help with following
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Apply your knowledge
Why are monosaccharides highly
soluble in water?
Why do monosaccharides have high
boiling and melting points?
Identify carbons 3 and 5 in the
monosaccharides below
9
Reducing & non - reducing sugars (
Learning goal 5)
A classification that helps differentiate
monosaccharides
Reducing sugars
Also known as aldoses. E. g. glucose
Changes Benedicts solution from
)
blue to red
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Question:-
How do the levels of structure achieved in proteins?
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Algebra Homework
les: Lipids D O
Add-ons Help
Last edit was seconds ago
Arlal
BIUA
三, = E▼m、回
11
3. What are the monomers?
4. What are the polymers?
5. Describe the shape/structure of a lipid (triglyceride). You may add a picture as an example, but be sure
describe it.
5. What are the differences between saturated fats and unsaturated fats? (words and pictures)
. Describe the function of lipids in the human body.
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Check all applied
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Show all working explaining detailly each step
Solution should be typewritten with a computer keyboard!
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1
peg
Part I: Fill in the Blank: Match one term from the word bank below which best completes each statement. 1pt
each.
1. This term refers to the dietary fiber which most animals cannot digest, however it keeps your digestive
system healthy!
2. Cholesterol is an important substance in the body. It is a type of
3. The building blocks of proteins are
4.
are molecules whose specific function are to speed up reactions in the body. They act as
catalysts for biologic reactions.
5. Adenine (A), Guanine (G), Uracil (U) and Cytosine (C) are all nucleotide bases for this molecule:
6. Lipids are
and the non-polar nature of the carbon-hydrogen bonds.
7. Structure and
meaning they are "water-fearing". This is due to the long hydrocarbon chains
always go together in biology, especially when we talk about proteins!
Word Bank: Use the following to complete the matching above.
Basic
Atomic Number
Neutral
Lactose
Amino Acids
Proteins
Energy
Acidic
Mass Number
Sucrose
DNA
Steroid
Enzymes
Double Helix…
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Coursework- Take Test Vie.. x
Lecture 2 Quiz
Time limit:
Length:
Scored out of:
Lecture Quiz in Lecture Quizzes
No time limit
10 questions
13 Points
Time Remaining:
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True
O False
7) Which level of protein structure is when the protein is actually capable of being
(1pt
functional?
O Primary
O Secondary
O Tertiary
All of the above
None of the
above
8) When a protein is not functional, it is said to be
(1pts)
O Type here to search
ロロ
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B.
Q8.
Unanswered
Q8. Hydrogen bonds between parts of the macromolecule are involved in producing which of the
following? (choose all that apply)
O Select all that apply
primary structure of proteins
shape of fats
secondary structure of proteins
D.
tertiary structure of proteins
structure of cellulose
E.
1 Submit
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Mastering Biology Course Home x
3 MasteringBiology: Macromolecul X
session.masteringbiology.com/myct/itemView?assignmentProblemlD=178811495
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lacromolecules and Membranes
apter 8 Question 8
Complete the hypothesis that explains these results.
Match the terms in the left column to the appropriate blanks in the sentences on the right.
Reset Help
concentration gradient
Sucrose and H move together into the plant cell through a(n)
with
H+
moving up a(n)
and
moving down a(n)
sucrose
The H gradient is maintained by a(n)
proton pump, which requires
АТР
cotransport protein
electrochemical gradient
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Course Code: BIO-121
Chapter 3: Molecules of Life
Course Name: Principles Of Biology-1
2.
State the difference between a saturated and unsaturated fatty acid.
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biochemistry
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- las 2 act 3 and guide questionarrow_forwardCourse Code: BIO-121 Chapter 3: Molecules of Life Course Name: Principles Of Biology-1 5. State the differences between starch and glycogen.arrow_forwardExercise B: Peptide Bond Formation Figure 2 shows two individual amino acids, and then those same two amino acids after they have been linked together by a peptide bond to form a dipeptide. Addition of more amino acids linked by peptide bonds would form a polypeptide, the precursor to a functional protein. нн +| | || H-N-C-Ĉ-0 H. +! | || H-N-C-ċ –0 H. H H H +| | || H-N-C-C-N-C-C- + H CH2 CH2 H CH2 H. CH2 SH SH NH, NH, Figure 2. Formation of a peptide bond between two amino acids. Answer the below questions in your own document. 1. Which two amino acids are shown on the left side of Figure 2? Use the Figure 3.2 from your text to answer this. 2. To which chemical groups do these amino acids belong? 3. Were you able to identify their chemical characteristics based on your rules? If not, you should go back and revise your rules! On the dipeptide shown in Figure 2, label the peptide bond that was formed when the two individual amino acids were joined. Label the free amino and carboxyl…arrow_forward
- Exercise B: Peptide Bond Formation Figure 2 shows two individual amino acids, and then those same two amino acids after they have been linked together by a peptide bond to form a dipeptide. Addition of more amino acids linked by peptide bonds would form a polypeptide, the precursor to a functional protein. H H H. H H +| | H-N-Ċ- ċ-0 H-N-Ć- Ĉ-O H-N-Č -C. N-C-C- H CH2 H. CH2 H. CH2 H CH2 SH SH NH2 NH2 Figure 2. Formation of a peptide bond between two amino acids. Answer the below questions in your own document. F1. Which two amino acids are shown on the left side of Figure 2? Use the Figure They 3.2 from your text to answer this. 2. To which chemical groups do these amino acids belong? 3. Were you able to identify their chemical characteristics based on your rules? If not, you should go back and revise your rules! On the dipeptide shown in Figure 2, label the peptide bond that was formed when the two individual amino acids were joined. Label the free amino and carboxyl groups at the ends…arrow_forwardExercise B: Peptide Bond Formation Figure 3 shows two individual amino acids, and then those same two amino acids after they have been linked together by a peptide bond to form a dipeptide. Addition of more amino acids linked by peptide bonds would form a polypeptide, the precursor to a functional protein. нн H H O нно H O +| | || H-N-C-ċ-o + +| 1 || H-N-C-C +| | || Н-N—С- С—N—C—С H CH2 H CH2 H CH2 CH2 SH SH NH2 NH2 Figure 3. Formation of a peptide bond between two amino acids. Answer the below questions in your own document. • Which two amino acids are shown on the left side of Figure 3? Use Figure 2 to answer this. • To which chemical groups do these amino acids belong? Were you able to identify their chemical characteristics based on your rules? If not, you should go back and revise your rules! On the dipeptide shown in Figure 3, label the peptide bond that was formed when the two individual amino acids were joined. Label the free amino and carboxyl groups at the ends of this…arrow_forwardNeed help on questions 3, 4, and 5.arrow_forward
- Learning Objectives Identify a peptide bond, the N-terminus (amino-terminus) and C- terminus (carboxyl-terminus) of a polypeptide in a series of linked amino acids. Describe the four levels of protein structure (primary, secondary, tertiary, and quaternary), what types of bonding interactions hold each level together, and how a protein’s structure relates to its cellular function. Link the chemical structures of amino acid R groups to the types of interactions they could form in the folded structure of a protein. Hypothesize the likely consequence of environmental conditions on the folded structure. Recognize secondary structure elements when proteins are represented in different ways (e.g. ball-and-stick structures, ribbon diagrams). Define these terms: enzyme, enzyme activity, active site, substrate, enzyme substrate complex, product, denature. Explain with molecular detail how some conditions affect enzyme activity.arrow_forwardACTIVITY 12 - LIPIDS As you watch the video, take notes about what you are learning about lipids. Images have been provided to help you think about the information you are hearing. Triglycerides are made from a glycerol and 3 fatty acids. shutterst beck Phospholipids are important in the structure of cells. Cholesterol is used many ways in the body.arrow_forwardB14U A Goals n Skills Minds On Actio O Connect 2 Choose any two words in the table below, then connect them with a complete idea. Repeat this process three times in total. monomer disaccharide glucose cell wall energy structure glycosidic bond isomer cell-to-cell communication For example: if the two words are ribosome and protein, then you could write: Ribosomes are connected to proteins because the ribosomes are the protein builders in the cell. Ribosomes are made of two parts or subunits. The larger of the 2 parts is where the ribosome can add on an amino acid to the growing protein chain. Practice good Organization skills by reviewing concepts and vocabulary from the whole Activity to include full details. Choose your best idea and share it with your classmates. Join The Discussionarrow_forward
- BIOCHEMISTRY please helparrow_forwardPlease help with these quickly.arrow_forwardBiomolecules Pre-Assessment One similarity between carbohydrates and lipids is they both... O contain nitrogen as part of their structure. O are composed of fatty acid chains. are made up of chains of smaller subunits. act as enzymes and contain peptide bonds.arrow_forward
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