Ch. 5 Molecules of Life – Test Study Guide
Carbohydrates, Fats, & Proteins: For all three groups
-Which molecules react well with water - hydrophilic? Which molecules do not mix well with
water- hydrophobic?
-Which molecules are polar? Which are nonpolar?
-What are the monomers of each? How does the molecule progress to become a polymer?
-How does dehydration synthesis work to the build a polymer of each group?
-What kind of bond / elements are involved with each type of bond to make a polymer?
-How does hydrolysis work to break down the polymer of each group?
-What are examples of chemical formulas for each of the groups?
-What are the common and scientific names for each group?
-What substances below to what groups – for example starch, hormones, glycerol?
-What are the different functions of each group (carbohydrates for energy and so on)
-Which and how are these groups listed on a food label?
Chemistry
-What does it mean to be an organic molecule?
-What is an ion? What is an isotope?
-What is an ionic bond? What is a covalent bond?
-What is the pH range of an acid, alklaline, and neutral?
-What are the chemical structures and chemical reactivity (water interaction, polarity,
acid/base) for each of the following functional groups: hydroxyl, carboxyl, amino, ketone,
aldehyde, phosphate, nitrogen with lone pair electron.
-Use a chart to determine what food types are present based on lab data.
-Draw the isomers and stereoisomers of C2H4O. What are the similarities and differences
between isomers and stereoisomers.
Carbohydrates
-Be able to identify alpha and beta glucose and fructose forms.
-What are the different forms and functions of a polysaccharide
Fats
-How can you tell the difference between a phospholipid and triglyceride?
-How can you tell the difference between saturated, monounsaturated, and polyunsaturated
fats.
-Explain the health factors related to cholesterol and fat saturation.
Proteins
-Predict the reactivity of an amino acid based on it R-groups, 4 sub-groups.
-Draw the basic structure of amino acid as neutral and as a zwitter ion.
-What are the 4 types of protein structures? What mechanisms are in place to cause the shape
at each level.
-How would a row of amino acids form a secondary protein structure based on its functional
groups?
Enzymes
-How can one increase the rate of an enzymatic reaction?
-Interpret a graph on the effects of different enzymes.
-What is a catalyst and how is it affected in a chemical reaction?
-What is the general formula for an enzymatic reaction?
-Explain how the induced fit model works using sucrase and sucrose as an example.
-What is denaturation of an enzyme – how does it occur?
Essays
1. Be able to draw the isomers and stereoisomers of a given formula. (From above C2H4O)
2. Draw and explain the dehydration synthesis between two given amino acids.
3. Draw and explain the hydrolysis of maltose.
4. Be able to apply the terms of enzyme, substrate, enzyme-substrate-complex, and
products to a given scenario like sucrase + sucrose  fructose + glucose + sucrase
ANSWERS for Biochem Unit Test Study Guide
Category
React with water
Carbohydrates
Hydrophilic
Fats
Glycerol – polar
Fatty acids- nonpolar
Polarity
Polar – OH groups
Monomers
Polymers
Monosaccharide polysaccharide
Glycerol – polar
Fatty acids- nonpolar
Glycerol & fatty acids
 triglyceride.
Dehydration
synthesis & bonds
Remove 1 water to
make a disaccharide
from 2
monosaccharides
Polysaccarides 
Monosaccharides
Remove 3 water
molecules to bind
glycerol with 3 fatty
acids
Triglyceride 
Glycerol + 3 fatty
acids
Glucose- C6H12O6
Gycerol- C3H8O3
Linoleic acidC18H32O2
fats, oils
Hydrolysis
Chemical formula
examples
Common names/ food Sugars, syrups
Functions
1.Energy for body
2.Stored energy
1.Stored energy
2.Cell membranes
Food Label
Carbohydrates,
sugars
Fats, saturated,
cholesterol
Proteins
Amino acids – depends
on R group:
hydrophobic /
hydrophilic / acid /
base
Amino acids – polar r
groups
Amino acids 
polypeptide chains 
primary, secondary,
tertiary, quarternary
Remove 1 water
molecule to make a
peptide bond
4th structure 3rd
structure  2nd
structure
polypeptide chain 
amino acids
Serine- C3H7NO3
meats, legumes
(beans)
1.Structures- hair,
muscle, tissues
2.Hormones &
enzymes
Proteins
Chemistry
-What does it mean to be an organic molecule? Has carbon and hydrogens
-What is an ion? What is an isotope? Ion- positively or negative charged element or
molecule. Isotope- heavier form of an element – has more neutrons.
-What is an ionic bond? What is a covalent bond? Ionic bond- one element gives up an
electron to another element – creating a positive and negative charge. The elements then
attract due to opposite charges. Covalent bonds- valance electrons are shared between
two elements outer shell of electrons.
-What is the pH range of an acid, alklaline, and neutral? Neutral – 7, Acid 0-7, Alkaline / base
7-14
-What are the chemical structures and chemical reactivity (water interaction, polarity,
acid/base) for each of the following functional groups: hydroxyl, carboxyl, amino, ketone,
aldehyde, phosphate, nitrogen with lone pair electron.
Hydroxyl- hydrophilic, polar
carboxyl-hydrophilic / acidic,
amino- alkaline /
hydrophilic,
ketone- hydrophilic/polar
aldehyde-hydrophilic/ polar
phosphate- polar / hydrophilic,
nitrogen with lone pair electron- alkaline /polar
-Use a chart to determine what food types are present based on lab data.
-Draw the isomers and stereoisomers of C2H4O. What are the similarities and differences
between isomers and stereoisomers.
Carbohydrates
-Be able to identify alpha and beta glucose and fructose forms.
Glucose- has a six carbon ring structure; fructose has a 5 carbon ring structure. For alpha
forms the Hydroxyl group on the 1st carbon is down. For beta forms the hydroxyl is up.
-What are the different forms and functions of a polysaccharide
Glycogen- branched chain stored energy for glucose
Cellulose- structural support in stems of plants
Starch- complex sugar food source found in potatoes, rice, and corn
Fats
-How can you tell the difference between a phospholipid and triglyceride?
Phospholipids have two fatty acid tails and a phosphate in the glycerol– triglycerides
have three fatty acid tails
-How can you tell the difference between saturated, monounsaturated, and polyunsaturated
fats. Saturated- have no C=C double bonds and all C are saturated with H atoms.
Monounsaturated- have one C=C double bond, and polyunsaturated has two or more C=C
bonds.
-Explain the health factors related to cholesterol and fat saturation.
Saturated fats and LDL cholesterol lead to clogged arteries. Unsaturated fats and HDL are
healthier choices of fats for a human diet.
Proteins
-Predict the reactivity of an amino acid based on it R-groups, 4 sub-groups.
1. Non-polar, hydrophobic – not interact due to carbons all full of hydrogens
2. Polar, hydrophilic- interacts in water due to the hydroxyl group
3. Acidic- the carboxyl group will release a H+ ion when in water – increasing the pH
4. Alkaline- the nitrogen with a lone pair of electrons will pull a hydrogen ion to it when
in water – increasing the pH of water (more OH- than H+)
-Draw the basic structure of amino acid as neutral and as a zwitter ion.
-What are the 4 types of protein structures? What mechanisms are in place to cause the shape
at each level. See notes: Primary- polypeptide; Secondary-alpha helix and beta-pleated
sheets; Tertiary- Ionic bonds, sulfur bridges, hydrophobic reactions, hydrogen bonds;
Quarternary- multiple amino acids form protein structure.
-How would a row of amino acids form a secondary protein structure based on its functional
groups? See above 4 types of amino acids. Hydrophobic on inside, hydrophilic on outside.
Enzymes
-How can one increase the rate of an enzymatic reaction? Place in ideal temperature and pH.
-Interpret a graph on the effects of different enzymes.
-What is a catalyst and how is it affected in a chemical reaction? Catalyst speeds up a reaction
without being broken down.
-What is the general formula for an enzymatic reaction? E + S --> ES --> E + P
-Explain how the induced fit model works using sucrase and sucrose as an example.
Sucrase (enzyme) binds to sucrose (substrate)  (products) glucose and fructose
+sucrase (enzyme)
-What is denaturation of an enzyme – how does it occur? Protein breaks down and unfolds
due to extreme temperature and pH changes.