Section 1 — Biological Molecules (Descriptive)

1. Define carbohydrates and describe their general roles in living organisms. Include
examples of simple and complex carbohydrates and how their structures relate to
their functions.

● Carbohydrates are organic molecules composed of carbon, hydrogen, and oxygen,

typically in a H:O ratio of about 2:1. They provide immediate and stored energy and
serve as structural components. Simple carbohydrates (monosaccharides) include
glucose, fructose, and galactose; disaccharides such as sucrose, maltose, and
lactose are formed from two monosaccharides; complex carbohydrates
(polysaccharides) include starch, glycogen, and cellulose. The soluble
monosaccharides and disaccharides supply quick energy, while polysaccharides
store energy (starch in plants, glycogen in animals) or provide structural material
(cellulose in plant cell walls). The specific linkages (alpha vs beta glycosidic bonds
and branching) determine digestibility and function.

2. Explain the differences between monosaccharides, disaccharides, and

polysaccharides. Give at least two examples of each category and describe how the
bonds between monosaccharides determine digestibility and function.

● Monosaccharides: single sugar units, e.g., glucose, fructose. They are the simplest
carbohydrates and are readily absorbed in the gut.

● Disaccharides: formed from two monosaccharides joined by a glycosidic bond, e.g.,

sucrose (glucose + fructose), maltose (glucose + glucose).

● Polysaccharides: long chains of monosaccharide units, e.g., starch (plant storage;

mostly glucose linked by α-1,4 and α-1,6 bonds), glycogen (animal storage; highly
branched α-1,4 and α-1,6 bonds), cellulose (plant structure; β-1,4 bonds not
digestible by humans). Digestibility depends on the type of glycosidic bond: α-bonds
are generally digestible by human enzymes, while β-bonds (as in cellulose) are not,
giving cellulose a structural role.

3. Describe the structure of starch, glycogen, and cellulose. Compare their roles in
plants vs animals and explain why humans can digest some but not others.

● Starch: a mixture of two polysaccharides, amylose (unbranched α-1,4) and

amylopectin (branched α-1,4 and α-1,6). It is the main storage carbohydrate in plants.

● Glycogen: highly branched polysaccharide with α-1,4 and α-1,6 linkages; the storage
carbohydrate in animals.

● Cellulose: linear polymer of β-1,4-linked glucose units; forms rigid dietary fiber in
plant cell walls.

● Humans digest starch and glycogen with enzymes like amylase and maltase, which
cleave α-glycosidic bonds, providing energy. Cellulose’s β-1,4 bonds resist human
 enzymatic digestion, so it serves as dietary fiber aiding digestion rather than a source
of glucose.

4. Outline the tests used to identify reducing sugars, starch, fats, and proteins
(Benedict’s, iodine, ethanol emulsion, Biuret). For each test, state what a positive
result looks like and why.

● Reducing sugars (Benedict’s test): Benedict’s solution (copper(II) sulfate) plus heat;
positive result is a color change from blue to green/yellow/orange/red with a brick-red
precipitate, indicating reducing sugars donate electrons to reduce copper(II) to
copper(I) oxide.

● Starch (Iodine test): Add iodine solution; a blue-black color indicates the presence of
starch due to iodine fitting into the helical starch structure.

● Fats (Ethanol emulsion test): Mix fat with ethanol, then add water; a cloudy white
emulsion indicates fats/oils present due to dispersed fat droplets forming an
emulsion.

● Proteins (Biuret test): Add sodium hydroxide and copper sulfate; a violet or purple
color indicates peptide bonds present in proteins.

5. Explain the biochemical significance of water in cells, including solvent properties,

temperature regulation, and participation in reactions. Include a note on hydrogen
bonding and cohesion.

● Water is the universal solvent in biological systems; many solutes dissolve in water
due to its polarity, enabling transport and chemical reactions. It participates in
hydrolysis and condensation reactions. Water stabilizes temperature through high
specific heat and high heat of vaporization, which buffers organisms against rapid
temperature changes. Hydrogen bonds among water molecules create cohesion and
surface tension, supporting processes like capillary action and turgor pressure in
plants.

6. Explain what nucleotides are and summarize the basic structure of DNA, including
the four bases and base-pairing rules. Discuss how the sequence encodes genetic
information.

● Nucleotides are the monomers of nucleic acids, composed of a sugar (deoxyribose in

DNA), a phosphate group, and a nitrogenous base. DNA comprises two
polynucleotide strands forming a double helix; bases are adenine (A) pairs with
thymine (T), and cytosine (C) pairs with guanine (G). The sequence of bases
encodes genetic information by specifying the order of amino acids in proteins,
regulatory sequences, and other functional elements.

Section 2 — Enzymes (Descriptive)

7. Define an enzyme and explain why it is considered a biological catalyst. Include a
description of the active site and the enzyme–substrate complex.

● An enzyme is a protein that acts as a biological catalyst, accelerating chemical

reactions without being consumed. The active site is a specific region on the enzyme
with a shape complementary to the substrate; when the substrate binds, an
enzyme–substrate complex forms, lowering the activation energy and transforming
the substrate into products. The enzyme is unchanged after the reaction and can
catalyze multiple cycles.

8. Describe how enzyme activity can be affected by temperature and pH. Explain what
happens at the molecular level when conditions move away from the optimum and
how this impacts the active site.

● Enzyme activity increases with temperature up to an optimum, after which heat

causes denaturation due to disruption of non-covalent bonds, altering the active site
and reducing activity. Deviations from the optimum pH can also denature the enzyme
or alter ionization of amino acid residues at the active site, changing its shape and
substrate-binding ability. Extreme conditions disrupt the tertiary structure, preventing
substrate alignment and catalysis.

9. Differentiate between the terms active site, substrate specificity, and enzyme
denaturation. Give an example of a real enzyme and its substrate.

● Active site: the pocket or groove where the substrate binds; specificity arises from the
precise shape and chemical environment of the active site (e.g., maltase active site
binds maltose). Substrate specificity means each enzyme catalyzes a specific
substrate or group of related substrates. Denaturation is the loss of secondary,
tertiary, and quaternary structure, leading to loss of activity. Example: Amylase acts
on starch (starch substrate) to produce maltose.

10. Explain the concepts of anabolic versus catabolic reactions and give an example of
each in the context of digestion or metabolism.

● Anabolic reactions build larger molecules from smaller ones (e.g., protein synthesis
from amino acids; glycogen synthesis from glucose). Catabolic reactions break down
large molecules into smaller units to release energy (e.g., digestion of starch to
maltose by amylase; breakdown of glycogen to glucose during fasting).

11. What are cofactors and coenzymes? Provide examples and explain why they are
essential for some enzyme-catalyzed reactions.

● Cofactors are inorganic ions (e.g., Mg2+, Zn2+) that assist enzyme activity.
Coenzymes are organic molecules (often vitamins or vitamin-derived) that participate
in the reaction (e.g., NAD+ in redox reactions, FAD, coenzyme A). They’re essential
for enabling certain enzymes to function, often by aiding in substrate binding or
electron transfer.
 12. Discuss enzyme inhibition with at least two different types (competitive and
non-competitive). Describe how inhibitors interact with enzymes and the potential
physiological consequences.

● Competitive inhibition occurs when an inhibitor resembles the substrate and

competes for binding at the active site, reducing rate until substrate concentration is
high enough to outcompete the inhibitor. Non-competitive inhibition occurs when an
inhibitor binds to an allosteric site, changing the enzyme’s conformation and reducing
activity regardless of substrate concentration. In physiology, inhibitors can regulate
metabolic pathways or be the mechanism of action for drugs or poisons.

13. Explain the lock-and-key model and briefly contrast it with induced-fit. Include a
simple diagram in words if you like (no drawings required).

● Lock-and-key: the substrate fits exactly into the enzyme’s active site as a perfect
match. Induced-fit: binding of the substrate induces a slight change in the enzyme's
active site to better accommodate the substrate, improving catalysis. Both models
describe substrate positioning and activation, with induced-fit allowing more flexibility.

14. Describe how enzyme activity can be measured qualitatively in a laboratory setting
and why a quantitative measure (like rate) might be more informative.

● Qualitative measures include observing color changes or appearance of a precipitate

indicating product formation. Quantitative measures involve tracking product
formation or substrate consumption over time (rate) using spectrophotometry, pH
changes, or oxygen production, which provide kinetic data and allow comparison of
conditions (temperature, pH, inhibitors).

Section 3 — Integration and Application (Descriptive)

15. Compare and contrast how carbohydrates and enzymes contribute to digestion in the
human body. Include the specific enzymes involved and the substrates they act on.

● Carbohydrates are broken down by carbohydrases such as amylase (saliva and

pancreas) acting on starch to maltose and other oligosaccharides; maltase, sucrase,
and lactase in the small intestine further hydrolyze disaccharides to monosaccharides
(glucose, fructose, galactose) that are absorbed. Enzymes maximize digestion
efficiency and regulate the pace of nutrient release.

16. Explain how the structure of cellulose differs from starch and glycogen, and discuss
the implications for digestibility in humans.

● Cellulose has β-1,4 glycosidic bonds, forming a straight, rigid chain that forms strong
fiber in plant cell walls. Humans lack cellulase to break β-glycosidic bonds, so
cellulose cannot be digested; it functions as dietary fiber aiding bowel movement.
Starch and glycogen have α-1,4 (and α-1,6 in branched forms) bonds that human
 enzymes can hydrolyze to glucose.

17. Describe how you would design a simple practical to test for a target enzyme activity
in a given sample (e.g., amylase activity on starch). Include controls, variables, and a
brief outline of steps.

● Outline: Hypothesis: amylase in sample catalyzes starch breakdown. Controls:

negative control without enzyme; positive control with known amylase; blank with
buffer only. Variables: enzyme presence (independent), substrate starch
concentration, temperature, and pH (controlled). Steps: incubate starch solution with
sample at optimum temperature; take samples at intervals; use iodine test to assess
starch presence (color change to blue-black when starch remains; clearing indicates
digestion). Record time to starch disappearance or measure reducing sugars with
Benedict’s test as a quantitative proxy.

18. Choose one topic from Biological Molecules or Enzymes and explain its relevance to
a real-world health issue (e.g., lactose intolerance, metabolic disorders, or enzyme
replacement therapy).

● Topic: Enzyme inhibitors and drug design. Relevance: enzyme inhibitors are used as
medicines to regulate metabolic pathways or treat diseases (e.g., protease inhibitors
in HIV therapy, acetylcholinesterase inhibitors in Alzheimer's treatment).
Understanding competitive and non-competitive inhibition helps explain how drugs
can modulate enzyme activity, minimize side effects, and improve therapeutic
outcomes.