BIOCHEMISTRY - UNIT 1 TEST REVIEW Daniel Nguyen

1. Covalent Bond: equal sharing of a pair of electrons

Ionic Bond: the transfer of electrons from one atom to another
Polar Covalent Bond: pair of electrons is shared unequally
Hydrogen Bond: forms between a molecule and another; between a hydrogen atom and one molecule of a highly
electronegative atom (oxygen, nitrogen, fluorine, etc.)
2. Water is a universal solvent because of its ability to dissolve a huge range of substances.
3. 1 mole = 6.02 x 1023 particles (atoms or molecules)
4. a) A pH scale indicates how acidic or base a solution is.
b) Acid: a substance that increases the H+ concentration of a solution
Base: a substance that reduces the H+ concentration in a solution
Buffer: a substance that minimizes changes in the concentration of H + and OH-
c) Bicarbonate buffer system
Step 1: Carbon dioxide release from tissue cells combines with water to form carbonic acid within the red blood
cells CO 2 + H2O  H2CO3
Step 2: The carbonic acid in the blood tends to dissociate into H+ ions and bicarbonate ions. These free H+ ions will
lower the pH of the blood (make it more acidic) and as a result, they must be removed.
H2CO3  H+ + HCO3-
Step 3: Hemoglobin reacts with the free H +. Acid hemoglobin (HHb) is weaker acid than carbonic acid. Thus, free H+
ions removed from solution and pH is not affected much. Once in lungs, CO 2 pressure lowered than that in blood.
Chemical reactions reserved and carbon dioxide gas released. H + + HCO3- +
K+ Hb- K+ + HCO3- + HHb
5. a) Redox reaction: transfer of electrons from one atom/molecule to another. A substance that loses an electron is
oxidized through oxidation. A substance that gains an electron is reduced through reduction.
b) Electrons transfer along with a proton (= 1 hydrogen atom)
c) LeO the lion goes GR!
6. Condensation (dehydration) reaction: involve the removal of a water molecule. Important in the formation of large
macromolecules from small molecules.
7. Hydrolysis reaction: involve addition of a water molecule. Important in the breaking of macromolecules into
smaller units.
8. Neutralization reactions: an acid and a base neutralize one another to form water and ions combined to form a
salt. Acid + base  water + salt
9. Endergonic reaction: chemical reactions that need an input of energy
Exergonic reaction: chemical reactions that release energy
10. Functional group: group of atoms with definite chemical properties
11. a) Macromolecule: extremely large molecules. Composite molecule: another type of molecule. Polymer: long chain
of similar components held by covalent bonds
b) 3 types of polymers: polysaccharides (polymer of sugars), proteins (polymer of amino acids), nucleic acids
(DNA/RNA) (polymers of nucleotides)
12. a) Carbohydrates – carbon, hydrogen, oxygen C:H:O is 1:2:1
b) C6H12O6, isomers: of each other because they are molecules with the same molecular formula but different
structural formula
c) Glucose made insoluble by making polysaccharides (long polymers of sugar resides)
d) Amylose – long unbranched chains of 60-300 units of glucose per chain. Pectin – branched polysaccharide of 300-
600 glucose units per chain
e) Starch found in humans is glycogen
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BIOCHEMISTRY - UNIT 1 TEST REVIEW Daniel Nguyen
f) The cellulose chains run parallel to one another in alternating layers to provide strength
g) Chitin is found in the exoskeletons of insects and crustaceans.
13. a) Two components of a fat or oil are: glycerol and fatty acids. Fats are oils are triglycerides because they consist of
one molecule of glycerol joined to 3 fatty acid molecules.
b) A C-H bond are found in fats and oils, the linkage that forms is called an ester linkage
c)

Fats Oils
Solid at room temp. Liquid at room temp.
Found in animals Obtained from plants
Converted to fat by saturating fatty acids with hydrogen
d) Saturated = line, solid; Unsaturated = kinks, liquid. Presence of double bonds produced ‘kinks’ in hydrocarbon
chain, causing them not to align themselves close to one another.

e)
f)

Phospholipids Triglyceride

Non-polar
hydrophobic

Amphipathic because it is a molecule with hydrophobic and

hydrophilic ends. This allows phospholipids to form
membranes.

14. a) Amino acid consists of: amino acid group (H-N-H), carboxyl group (O=C-OH), hydrogen atom(H), side chain (R)

b) The side chain distinguishes one amino acid from another.

c) A covalent bond, known as a peptide bond, holds amino acids together.
d) Dipeptide: molecule made of 2 amino acids. Tripeptide: molecule made up 3 amino acids. Polypeptide: molecule
made of more than 3 amino acids
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BIOCHEMISTRY - UNIT 1 TEST REVIEW Daniel Nguyen
e) Polypeptide chain has direction because the amino acids have different ends.
f) The four levels of protein structures are:
Primary structure: sequence of the amino acids in a polypeptide chain.
Secondary Structure: refers to the folding or coiling of the protein due to hydrogen bonding between amino acids
(e.g. Coiling gives rise to an α-helix, folding gives rise to a β-sheet)
Tertiary Structure: refers to the 3 dimensional shape of the protein, affected by interactions between side groups
on amino acids. Proteins may be fibrous or globular. (E.g. Disulphide bonds, ionic bridges, hydrogen bonds between
different regions)
Quaternary Structure: refers to the way chains (polypeptides) are packed together. This is restricted to proteins
composed of 2 of more polypeptide chains (subunits) (e.g. Hemoglobin – 4 polypeptide chains)
g) Denaturation of a protein: proteins will lose their characteristics and their functions
15. a) Nucleotides: consist of a five-carbon sugar (deoxyribose in DNA, ribose in RNA), a phosphate group, an organic
nitrogen-containing base
b) A phosphodiester bond holds nucleotides together
c) Nucleotide sequence of one strand of DNA determines the sequence of the other strand. (A-T C-G)
d)

DNA RNA
Sugar present  5-carbon sugar called deoxyribose sugar 5-carbon sugar called ribose
Nitrogenous bases  Adenine (A), thymine (T), cytosine (C), Adenine (A), uracil (U), cytosine (C),
guanine (G) guanine (G)
16. a) Enzymes are catalysts (a substance that speeds up a chemical reaction without being consumed in the process,
therefore making them reusable)
b) Substrate: the reactant that an enzyme acts upon when it catalyzes a chemical reaction
c) Catalysts speed up reactions by reducing the amount of activation energy (by stretching and bending bonds that
normally break in the reaction) needed for the reaction to occur.
d) Lock-and-Key Mechanism – substrate fits directly into the binding site of the enzyme
Induced Fit Mechanism – as substrate enters active sites, its function group reacts with the functional groups of
amino acids of the enzymes, causing the enzyme to change its shape to better fit the substrate
e) Competitive inhibitors – substances that compete with the substrate for an enzyme’s active site
Non-competitive inhibitors – substance that attach to a binding site on the enzyme other than the active site
causing a change in the enzyme’s shape and a loss of affinity (attraction force) for its substrate
f) Allosteric sites: receptor sites, some distance from the active site, which binds substances that may inhibit or
stimulate an enzyme’s activity
g) Protease: enzyme that breaks down proteins.

h)

i) Lactose-intolerance: people who lack lactase (enzyme that breaks down lactose)
j)

17. a) The activity increases as the substrate concentration or enzyme concentration increases. More substrate
molecules or enzyme molecules = increase in frequency of collisions between substrate and enzyme molecules.
More collisions leads to more effective collisions (proper place of substrate and enzyme’s active sites), therefore
rate of reaction increases.

Daniel Nguyen
BIOCHEMISTRY - UNIT 1 TEST REVIEW Daniel Nguyen
b) Low temperature = bonds rigid, collisions (due to slow molecular motion) is reduced, enzyme activity low.
Optimal temperature = increase in enzyme activity, increase in movement of enzyme and substrate molecules,
increase in number of effective collisions
High temperature = enzyme activity deceases due to denaturation of enzyme, the structure of the enzyme is
altered so it cannot bind substrate
18. a) Fluid-mosaic model of the cell membrane – consists of a phospholipid bilayer with proteins embedded in it.
‘Fluid’ because it is dynamic (lipid molecules and proteins can move freely) and double bonds lead to ‘kinking’
chains. Proteins distributed throughout membrane in a ‘mosaic’-like pattern
b) Diffusion: net movement of molecules to regions of lower concentration as a result of random, spontaneous
molecular motions
Osmosis: diffusion of water across a semi-permeable membrane (only allows certain molecules across)
c) Hypertonic solution – concentration of solutes is greater outside the cell, water diffuses out of cell
Hypotonic solution – concentration of solutes is greater inside the cell, water diffuses into the cell (plant cells
become turgid, stiff, animal cells burst), concentration of water greater outside cell
Isotonic Solution – concentration of solutes is the same inside and outside the cell (animal cells are normal, plant
cells flaccid (soft), concentration of water same inside cell
d) Endocytosis: process by which cells absorb molecules from outside by engulfing it with their cell membranes, by
vesicle formation
Phagocytosis: cells engulf organisms or fragments of organisms
Pinocytosis: cells engulf liquids containing dissolved materials
Exocytosis: reverse process in with materials are extruded
e) Facilitated diffusion: transport of molecules across a membrane by a carrier protein in the direction of lowest
concentration. Different than diffusion because it is specific, passive (follows gradient from area of high
concentration to an area of low concentration), prevents leakage, number of channels is a limiting factor
f) Active transport: transport of a solute across the cell membrane against the concentration gradient. It requires
energy to proceed, the energy comes from ATP.
19. Ribosomes
 small, almost spherical organelles made of ribosomal RNA (or rRNA) and proteins
 responsible for synthesizing proteins
Mitochondria
 rod shaped organelle called the ‘powerhouse’ of the cell because it supplies the cell with chemical energy
called ATP (adenosine triphosphate)
Endoplasmic Reticulum
 acts as a channel for the transport of cellular materials: provides surface area for enzymes to catalyze
chemical reactions especially those leading to protein synthesis
Golgi Apparatus (Golgi Body)
 acts as a centre of manufacturing, warehousing, sorting and shipping
Vacuoles
 are membrane-bound, fluid-filled sacs
 plant cell vacuole stores molecules such as amino acids, pigments, sugars, etc. and also stores hydrolytic
enzymes to digest macromolecules
Lysosomes
 contain strong digestive (hydrolytic) enzymes that act as the cell’s digestive system allowing for the
breakdown of proteins, polysaccharides, fats and nucleic acids (DNA/RNA)

Daniel Nguyen