Transcript Proteins, Lipids, and Carbs!!!

Proteins
OH MY!!!!
If molecule Y is a protein, molecules “W” are best
described as:
0%
0%
100%
0%
1.
2.
3.
4.
Nucleic acids
Carbonic acid
Amino acids
Fatty acids
The monomer unit pictured below
can best be describe as:
100%
0%
0%
0%
1.
2.
3.
4.
Amino acid
Carbohydrate
Nucleic acid
Fatty acid
Which of the following amino acids
would you expect to mix with water:
89%
0%
5%
5%
1.
2.
3.
4.
A and B
B and C
C and D
A and D
A
C
B
D
Which amino acids would form ionic
bonds:
A
0%
89%
11%
0%
1.
2.
3.
4.
A and B
B and C
C and D
A and D
C
B
D
When a dehydration reaction takes place between the
molecules below, a ___________ bond is
formed:
0%
95%
0%
5%
0%
1.
2.
3.
4.
5.
Polar
Peptide
Ionic
Hydrogen
Amino
…………………………………
…………………………………
….
Which bond type is called a
hydrogen bond?
68%
0%
32%
0%
1.
2.
3.
4.
A
B
C
D
d
a
b
c
The reaction pictured below (moving from
top to bottom) can best be described as
a(n):
0%
1. Hydrolysis
2. Dehydration
100%
3. Hydration
0%
4. Rehydration
0%
Which area(s) of this molecule
would be repulsed by water?
0%
39%
6%
56%
1.
2.
3.
4.
A
B
C
D
d
a
b
c
The part of the molecule outlined in
blue is best described as a:
1.
2.
3.
4.
Ionic bond
Covalent bond
Hydrogen bond
Peptide bond
The type of interaction at location
“B”
0%
17%
83%
0%
1.
2.
3.
4.
Ionic
Disulfide
Hydrophobic
hydrogen
B
C
A
D
The type of interaction at location
“E”
94%
0%
0%
6%
1.
2.
3.
4.
Ionic
Disulfide
Hydrophobic
hydrogen
B
C
A
D
E
The amino acid most likely at
location “D”
0%
6%
0%
94%
1.
2.
3.
4.
Alanine
Glycine
Valine
Cysteine
B
C
A
D
Let’s assume this is a single protein. The
highest level of protein structure pictured
here is:
0%
1. Primary
2. Secondary
0%
3. Tertiary
95%
4. Quaternary
5%
B
A
D
C
Structures A and B are known
respectively as:
0%
0%
0%
100%
1.
2.
3.
4.
Random coil; alpha helix
Alpha helix; random coil
Random coil; beta sheet
Alpha helix; Beta sheet
A
B
What level of protein structure is
shown below?
0%
20%
0%
80%
1.
2.
3.
4.
Primary
Secondary
Tertiary
Quaternary
TO DENATURE A PROTEIN
If the shape is changed so that it is no
longer able to perform its function, we
call it…
DENATURED
– What kinds of things do you think could
denature a protein?
Denaturation
a. Disruption of protein structure by
1. Heat: Break apart H bonds and disrupt
hydrophobic attractions
2. Acids/ bases: Break H bonds between polar
R groups and ionic bonds
3. Heavy metal ions: React with S-S bonds to
form solids
4. Agitation: Stretches chains until bonds
break
Applications of Denaturation
a.
b.
c.
d.
e.
Hard boiling an egg
Cooking food to destroy E. coli
Heat used to cauterize blood vessels
Autoclave sterilizes instruments
Milk is heated to make yogurt
Think about it
Tannic acid is used to form a scab on a burn.
An egg becomes hard boiled when placed in
hot water. What is similar about these two
events?
Solution
Acid and heat cause a denaturation of
protein. They both break bonds in the
structure of protein.
You are looking at the before and after
picture of a protein. Based on the picture,
what has happened to this protein:
0%
100%
0%
0%
1.
2.
3.
4.
The protein has become renatured
The protein has become denatured
The protein has reached its highest level of
organization
A
None of the above
B
Let’s Talk about….
•Enzymes
Based on the bonding between the
glucose molecules, this is most
likely :
0%
0%
0%
0%
1.
2.
3.
4.
Glycogen
Starch
Maltose
Cellulose
Which of the following would be a liquid at room
temperature due to the fact it is an unsaturated
fatty acid?
1.
2.
3.
4.
5.
0%
0%
0%
0%
0%
A
B
C
D
C and D
B
A
D
C
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2
3
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5
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I am used by the body in the production of
various hormones
1.
2.
3.
4.
0%
0%
0%
0%
A
B
C
D
B
A
D
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2
3
4
5
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25
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This molecule is best described as
a ____________
1.
2.
3.
4.
0%
0%
0%
0%
Monoglyceride
Diglyceride
Triglyceride
polyglyceride
1
2
1
2
3
4
5
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The final macromolecule we have
yet to discuss are the:
1.
2.
3.
4.
0%
0%
0%
0%
Nucleic acids
Nucleic acids
Nucleic acids
Nucleic acids
1
2
3
4
5
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25
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