Download Biomolecules Test Review -KEY

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Biomolecules Test Review -KEY
1. What are the 4 large categories of organic compounds that we call biomolecules?
Proteins
Carbohydrates
Lipids
Nucleic Acids
2. What are examples of each biomolecule?
Examples
Starch, glucose, Cellulose, Glycogen
Biomolecule (polymer)
Carbohydrate
Oils, waxes, fats, vitamins, steroids, cell
membranes
DNA, RNA, ATP
Lipids
Enzymes, Insulin, Antibodies,
Hemoglobin
Proteins
Nucleic Acids
3. How are monomers and polymers related?
Polymers are long chains of single units called Monomers.
4. What is the difference in dehydration synthesis and hydrolysis? Use monomer(s) and polymer(s) in
your explanation. In which process is water used? Released? – Dehydration Synthesis
During dehydration synthesis monomers are linked together by the removal of a water molecule
producing a polymer; which is the opposite of what occurs during hydrolysis. Hydrolysis adds water to
a polymer, breaking the bonds holding the polymer together, resulting in individual monomers.
5. What are the monomers for each biomolecule?
Monomer
Monosaccharide
Biomolecule (polymer)
Carbohydrates
Fatty Acids
Lipids
Nucleotides
Nucleic Acids
Amino Acids
Protein
6. What elements make up each type of biomolecule? (use the element’s symbol)
Elements
CHO
Biomolecule (polymer)
Carbohydrates
CHO
Lipids
CHONP
Nucleic Acids
C H O N sometimes S
Protein
Name:
7. How do you know C6H12O6 is a carbohydrate and not a lipid, protein, or nucleic acid?
Because the Hydrogen and Oxygen are in a 2:1 ratio and there is no N or P
8. Glucose, one type of monosaccharide, is represented by the chemical formula, C6H12O6. If you were to
put together 2 glucose molecules, why wouldn’t the molecular formula for the newly made
disaccharide be C12H24O12?
In order to link the 2 molecules together a water molecule must be removed (dehydration synthesis)
the resulting formula would be:
C6H12O6 + C6H12O6
C12H22O11 + H2O
9. What is the difference between saturated and unsaturated fatty acid? Which is better for you? Why?
Saturated fatty acid- single bonds, straight and tightly packed. Solid at room temperature. (Bad for us!)
Unsaturated fatty acid- double bonds bend the tails and it’s crooked (not straight). Liquid at room
temperature (ex. Olive Oil)
10. For proteins to function (work) they have to be folded in several conformations
A.
B.
C.
D.
Primary – sequence of amino acids
Secondary – coiled into a helix or pleat
Tertiary – folded into a “glob” that has an active site – it works in this shape
Quaternary – 2 or more tertiaries (globs) that are held together by a metal ion (i.e iron holds hemoglobin together;
copper holds myoglobin together)
What (molecule) directs or determines their primary conformation? DNA
11. When a protein is denatured, what does that mean? What can denature a protein (name 2)?
Denatured means that it changes shape and would no longer function properly.
Temperature and pH are 2 things that can denature a protein.
12. Nucleotides are the monomers of nucleic acids like DNA and RNA. What 3 things make up a
nucleotide? 1. 5-carbon sugar (pentose)
2. Phosphate group
3. Nitrogenous Base
13. Which nitrogenous base pairs bond together in deoxyribonucleic acid? Ribonucleic acid? How do they
differ?
Base Pairs
DNA
A–T
C-G
RNA
A –U
C-G
Name:
14. What are enzymes? How do they function? Enzymes are a catalyst. Catalysts are used to speed up a
reaction by decreasing the amount of energy needed to get the reaction started…Lowers the activation
energy.
15. What factors affect the rate at which enzymes function? Explain how each would affect the enzymes
rate of reaction.
Factors that Affect Rate at Which Enzymes Function
Temperature
How would it affect rate of reaction?
To hot or cold reaction would be inhibited
pH
pH to acidic or basic for that enzyme would
inhibit reaction
More enzymes the faster the substrate is
acted upon
Higher concentration would slow down total
reaction speed
Enzyme Concentration
Substrate Concentration
16. Using the diagrams shown: IDENTIFY and LABEL the active site, substrate, enzyme and product.
Substrate
Active Site
Products
Enzyme
Using the illustration above to describe what happens at each step:
Step 1: Substrate attaches to the enzyme at the active site (Like a lock and key it must be the right
shape in order to fit…doesn’t fit doesn’t work)
Step 2: Enzyme substrate complex formed – Reaction occurs
Step 3 (What happens to the enzyme?): Products are released from the enzyme. Enzyme remains
unchanged and is available to do the reaction again if more substrate is available.
17. Compare competitive and noncompetitive inhibition and how it affects enzyme function.
A noncompetitive inhibitor - is a substance that interacts with the enzyme, but usually not at the active site. The
noncompetitive inhibitor reacts either remote from or very close to the active site. The net effect of a noncompetitive inhibitor is to change the shape of the enzyme and thus the active site, so that the substrate can no
longer interact with the enzyme to give a reaction. Non-competitive inhibitors are usually reversible, but are not
influenced by concentrations of the substrate as is the case for a reversible competitive inhibitor.
A competitive inhibitor - is any compound which closely resembles the chemical structure and molecular
Name:
geometry of the substrate. The inhibitor competes for the same active site as the substrate molecule. The inhibitor
may interact with the enzyme at the active site, but no reaction takes place. The inhibitor is "stuck" on the enzyme
and prevents any substrate molecules from reacting with the enzyme. However, a competitive inhibition is usually
reversible if sufficient substrate molecules are available to ultimately displace the inhibitor. Therefore, the amount
of enzyme inhibition depends upon the inhibitor concentration, substrate concentration, and the relative affinities
of the inhibitor and substrate for the active site.
Name:
18. Complete the following chart:
Protein
Nucleic Acids
Carbohydrates
Lipids
Elements in
biomolecule
C, H, O, & N
Sometimes S
C, H, O, N, & P
C, H, O
Hydrogen and Oxygen (2:1)
C, H, O
Hydrogen and Oxygen
(greater than 2:1)
Where synthesized in
the cell
Function(s) of
biomolecule
Ribosome
Nucleus
Chloroplast
Smooth ER
Catalyst, Maintenance,
Repair, growth, transport,
and metabolism
Genetic Code
Blueprints of DNA
Cellular Energy
Short term energy storage
Structural support
Primary fuel source
Monomer
Amino Acids
Nucleotides
Examples
Meat, cheese, Milk
Insulin, Hemoglobin,
Antibodies, and Enzymes
RNA, DNA, & ATP
Monosaccharides (simple
sugars)
Potatoes, Rice, sugars
(glucose, sucrose, lactose, &
Fructose)
Cellulose, and Chitin
Long term energy storage
Cushion
Insulation
Vitamins
Steroids
Plasma Membranes
Fatty Acids
Fats, Oils, Waxes, Steroids,
& Vitamins
19. Where are the following digestive enzymes found and what are their roles in digestion?
Enzyme
Trypsin
Amylase
Pepsin
Lipase
Location
Small Intestine
Mouth/ Small Intestine
Stomach
Small Intestine
Role
Continues to break down Proteins
Breakdown simple sugars
Breaks down proteins into large peptides
Breaks down Lipids
Name:
20. Identify each of the following molecules
Carbohydrate
Nucleic Acid (ATP)
Lipid (Triglyceride)
Carbohydrate
Lipid (Saturated Fat)
Carbohydrate
Protein
Lipid (Unsaturated Fat)
Protein
Protein
Carbohydrate
Nucleic Acid
Lipid (phospholipid)