Biomolecules & Enzymes Review

1. Interpret rate of reaction graphs/diagrams and influence of enzyme substrate interactions.

 For a reaction to occur, you must overcome the activation energy (Ea)
 A lower “hump” on a graph equals a reaction taking place quicker.
 Enzymes speed up these reactions and reduce the Ea
2. Characteristics, properties, and types of bonds involved in protein structure.
 Proteins are made up of amino acids.
 Amino acids are composed of a basic amine group and an acidic carboxyl group and a radical
(R) group which makes the 20 different amino acids unique.
o Amino acids are acidic since the carboxyl group can release an H+ proton.
 Proteins are the most diverse biomolecule as they have the greatest number of functions
throughout the body.
 They act as enzymes, antibodies, hormones, receptors, transportation, motor, support, and
more.
 The bonds between amino acids are called peptide bonds.
 Proteins Structure:
1. Primary Sequence: the specific order of amino acids in a protein
2. Secondary Structure (the backbone): interactions between the bonds in the
amino acids
a. Helix (alpha)
b. Pleated Sheets (beta)
3. Tertiary Structure: interactions between the (R) groups
a. Globular
b. Fibrous
4. Quaternary Structure: 3 or more proteins interacting.
3. Define entropy and describe how it is affected in open and closed systems for different types of
reactions (i.e. endergonic, exergonic)
 Entropy  the measurement of a systems thermal energy per unit temperature that is
available for doing work. Also a measure of disorder/randomness since it is obtained from
molecular motion
 Open System  energy AND matter flowing in and out
o Entropy is decreasing
 Closed System  energy OR matter flowing in and out
o Entropy is increasing
 Endergonic Reaction  energy is being absorbed
 Exergonic Reaction  energy is being released
4. Polarity and solubility of the 20 amino acids used to make proteins.
 Polar amino acids have radical sidechains that include Nitrogen, Oxygen, or Sulfur
o Exception: Tryptophan and Methionine (both are nonpolar)
 Non-Polar amino acids have radical sidechains consisting of only Carbon and Hydrogen
 Polar amino acids are generally soluble in water as they have sidechains that form hydrogen
bonds with water molecules, allowing them to dissolve
5. Define Gibbs Free Energy
 Gibbs Free Energy (∆G) is the amount of available energy to do work, potential energy in
chemical reactions
 ∆G = ∆H – T∆S
o Where ∆H is the change in enthalpy (total energy of the system, measure of
heat/energy absorbed)
o Where T is the temperature in Kelvin
o Where ∆S is the change in entropy (measure of randomness in a system due to
molecular movement)
6. Understanding Free Energy changes (ΔG) in relation to: exergonic, spontaneous, endergonic,
non-spontaneous reactions.
 Spontaneous reactions are exergonic
o ∆G < 0
 Non-spontaneous reactions are endergonic since they require and absorb energy to occur
o ∆G > 0
7. Interpret free energy diagram for exergonic and endergonic reactions, including effect of
enzyme involvement in the reactions.

 Adding an enzyme to the reaction would lower the amount of energy needed to begin the
reaction and therefore speed up the process
 Endergonic  products favored (ex. Photosynthesis, since sunlight, an outside energy is
required)
 Exergonic  reactants favored (ex. Cell respiration, since ATP or energy is released)
8. Explain/define Keq and use it to describe endergonic and exergonic reactions and effect on
reaction pathways.
 Keq = [products] / [reactants]
 The value of Keq determines whether the reaction favours the products or the reactants and
therefore if the reaction is endergonic or exergonic
o If Keq > 1, the reaction is exergonic since products are favoured (energy is being released)
o If Keq < 1, the reaction is endergonic since reactants are favoured (energy is absorbed)
9. Condensation and hydrolysis reactions for carbohydrates, proteins, and triglycerides
(triacylglycerols/fats).
 Carbohydrates:

o Two chairshaped glucose molecules bond together to create a disaccharide and one
water molecule
o OH location memory: down, down, up, down, up
 Starting at Carbon 1, or to the right of the oxygen molecule
o The two glucoses form a bond at carbon 1 on the first molecule and carbon 4 on the
second
 Proteins:

o Two amino acids combine to form a dipeptide bond (protein) and a water molecule
o The aminos bind at the hydroxyl on the first amino to the amino on the second amino
acid
 This forms an N-C-C-N-C-C pattern
o All proteins start with an amino (NH2) and end with a carboxylic acid (COOH)

 Triglyceride:
 o Glycerol combines with 3 fatty acids chains to form triglyceride and 3 water molecules
o The triglyceride only change is removing all hydroxyl groups from the glycerol and each
Hydrogen atom from the hydroxyl on the fatty acids
o The fatty acids can be saturated (full of hydrogen, only single bonds) or unsaturated
(double bonds present)
10. Basic chemistry (i.e. composition of an atom, isotopes)
 Atoms are composed of positive protons and neutral neutrons in the nucleus and surrounded by
negative electrons
 Isotopes are atoms with the same number of protons but different number of neutrons
 REDOX Reactions:
o Oxidization is loss
o Reduction is gain
o The molecules oxidized = reducing agent
o The molecules reduced = oxidizing agent
11. Understanding biological molecules structure and function; recommended review of Biozone 1
pgs.51-54, 59-64.