🌍 Pre-Clinical · subject

Pre-Clinical Biochemistry Syllabus

The Biochemistry syllabus for Pre-Clinical in full: 8 chapters, 23 topics and 75 sub-topics, every one listed below, plus 51 Biochemistry flashcards with answers.

8Chapters

23Topics

75Sub-topics

51Flashcards

Biochemistry syllabus: all 8 chapters

Expand any chapter to see its topics and sub-topics.

Introduction to Biochemistry
2 topics
- Scope and Importance
  - Definition of Biochemistry
  - Applications in Medicine
  - Historical Development
- Cell Structure and Functions
  - Cell Membrane
  - Organelles
  - Cytoskeleton
Proteins
3 topics
- Amino Acids
  - Structure and Classification
  - Essential and Non-Essential Amino Acids
  - Peptide Bonds
- Protein Structure
  - Primary Structure
  - Secondary Structure
  - Tertiary Structure
  - Quaternary Structure
- Protein Function
  - Enzymes
  - Transport Proteins
  - Structural Proteins
  - Signaling Proteins
Enzymes
3 topics
- Classification
  - Oxidoreductases
  - Transferases
  - Hydrolases
  - Lyases
  - Isomerases
  - Ligases
- Mechanism of Action
  - Active Site
  - Enzyme-Substrate Complex
  - Catalytic Mechanisms
- Factors Affecting Enzyme Activity
  - Temperature
  - pH
  - Substrate Concentration
  - Inhibitors
Carbohydrates
3 topics
- Classification
  - Monosaccharides
  - Disaccharides
  - Oligosaccharides
  - Polysaccharides
- Metabolism
  - Glycolysis
  - Gluconeogenesis
  - Glycogen Metabolism
  - Pentose Phosphate Pathway
- Regulation
  - Hormonal Regulation
  - Allosteric Regulation
Lipids
3 topics
- Classification
  - Fatty Acids
  - Triglycerides
  - Phospholipids
  - Steroids
- Metabolism
  - Beta-Oxidation
  - Fatty Acid Synthesis
  - Cholesterol Metabolism
  - Lipoprotein Metabolism
- Clinical Aspects
  - Hyperlipidemia
  - Atherosclerosis
  - Obesity
Nucleic Acids
3 topics
- DNA Structure and Function
  - Double Helix
  - DNA Replication
  - DNA Repair
- RNA Structure and Function
  - Types of RNA
  - Transcription
  - RNA Processing
- Gene Expression
  - Genetic Code
  - Translation
  - Regulation of Gene Expression
Vitamins and Minerals
3 topics
- Fat-Soluble Vitamins
  - Vitamin A
  - Vitamin D
  - Vitamin E
  - Vitamin K
- Water-Soluble Vitamins
  - Vitamin B Complex
  - Vitamin C
- Minerals
  - Macrominerals
  - Microminerals
Metabolism Integration
3 topics
- Energy Balance
  - ATP
  - Energy Yield of Macronutrients
- Metabolic Pathways
  - Catabolic Pathways
  - Anabolic Pathways
- Hormonal Regulation
  - Insulin
  - Glucagon
  - Thyroid Hormones

Pre-Clinical Biochemistry flashcards — 51 questions with answers

What is biochemistry and why is it important in the medical curriculum?
Biochemistry is the study of the chemical processes and molecules within living organisms. It is important because it explains normal metabolism, the molecular basis of disease, drug action, and provides the foundation for diagnostic biochemical tests.
List the four major classes of biomolecules studied in biochemistry.
Carbohydrates, lipids, proteins, and nucleic acids.
Which cell organelle is the primary site of ATP production and why is it called the powerhouse of the cell?
The mitochondrion; it houses the electron transport chain and oxidative phosphorylation, generating most cellular ATP.
What are the functions of the rough and smooth endoplasmic reticulum?
Rough ER (studded with ribosomes) synthesizes and folds secretory/membrane proteins; smooth ER synthesizes lipids and steroids, stores calcium, and detoxifies drugs.
What is the role of the Golgi apparatus in the cell?
It modifies (e.g., glycosylation), sorts, and packages proteins and lipids into vesicles for secretion or delivery to other organelles.
What is the function of lysosomes and which enzymes do they contain?
Lysosomes are the cell's digestive organelles; they contain acid hydrolases (proteases, lipases, nucleases, glycosidases) active at acidic pH (~4.5–5) that degrade macromolecules.
Describe the fluid mosaic model of the plasma membrane.
The membrane is a fluid phospholipid bilayer in which proteins (integral and peripheral), cholesterol, and glycolipids are embedded and can move laterally, forming a dynamic mosaic.
What is the general structure of an amino acid at physiological pH?
A central α-carbon bearing a protonated amino group ($\ce{-NH3^+}$), a deprotonated carboxyl group ($\ce{-COO^-}$), a hydrogen, and a variable R side chain — existing as a zwitterion.
What is the isoelectric point (pI) of an amino acid and how is it calculated for a neutral amino acid?
The pI is the pH at which the molecule carries no net charge. For a neutral amino acid it is the average of the two relevant pKa values: $$pI = \frac{pK_{a1} + pK_{a2}}{2}$$
Name the amino acids classified as essential in humans.
Phenylalanine, Valine, Threonine, Tryptophan, Isoleucine, Methionine, Histidine, Arginine (semi-essential), Leucine, and Lysine (mnemonic: PVT TIM HALL).
Which amino acids contain sulfur, and which contains a secondary amine (imino) group?
Sulfur-containing: cysteine and methionine. Proline contains a secondary amine (it is technically an imino acid).
What bond links amino acids in a protein, and how does it form?
A peptide bond — an amide linkage formed by a condensation (dehydration) reaction between the α-carboxyl of one amino acid and the α-amino of the next, releasing water.
Define the four levels of protein structure.
Primary: linear amino acid sequence. Secondary: local folding (α-helix, β-sheet) stabilized by hydrogen bonds. Tertiary: overall 3D fold of one polypeptide. Quaternary: assembly of multiple subunits.
Compare the α-helix and β-pleated sheet.
α-helix: right-handed coil stabilized by hydrogen bonds between residues i and i+4, ~3.6 residues per turn. β-sheet: extended strands hydrogen-bonded side by side, either parallel or antiparallel.
Which bonds/interactions stabilize the tertiary structure of a protein?
Hydrophobic interactions, hydrogen bonds, ionic (salt) bridges, van der Waals forces, and covalent disulfide bonds (between cysteines).
What is protein denaturation and which structural levels does it disrupt?
Denaturation is loss of native 3D structure (secondary, tertiary, quaternary) due to heat, pH extremes, or chaotropic agents, while leaving primary structure (peptide bonds) intact; it usually abolishes function.
Explain the difference between fibrous and globular proteins with examples.
Fibrous proteins are elongated, structural, and insoluble (e.g., collagen, keratin). Globular proteins are compact, roughly spherical, and functional/soluble (e.g., hemoglobin, enzymes).
How does hemoglobin illustrate cooperative (allosteric) protein function?
Hemoglobin has 4 subunits; binding of $\ce{O2}$ to one subunit increases affinity of the others, producing a sigmoidal oxygen-binding curve (positive cooperativity).
What is the difference between the oxygen-binding curves of myoglobin and hemoglobin?
Myoglobin shows a hyperbolic curve (single high-affinity site); hemoglobin shows a sigmoidal curve due to cooperative binding among its four subunits.
What is an enzyme and what basic function does it perform?
An enzyme is a biological catalyst (usually a protein) that lowers the activation energy of a reaction, increasing its rate without being consumed or altering the equilibrium.

Show the other 31 Biochemistry flashcards

List the six IUBMB classes of enzymes.
Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases.
Distinguish a cofactor, a coenzyme, and a prosthetic group.
A cofactor is any non-protein helper (metal ion or organic). A coenzyme is a loosely bound organic cofactor (often vitamin-derived). A prosthetic group is a tightly/covalently bound cofactor (e.g., heme, FAD).
Explain the induced-fit model of enzyme action.
Substrate binding induces a conformational change in the active site so that it molds around the substrate, optimizing catalytic contacts — an improvement on the rigid lock-and-key model.
State the Michaelis–Menten equation and define its terms.
$$v_0 = \frac{V_{max}[S]}{K_m + [S]}$$ where $v_0$ is initial velocity, $V_{max}$ is maximum velocity, $[S]$ is substrate concentration, and $K_m$ is the substrate concentration at half $V_{max}$.
What does the Michaelis constant $K_m$ indicate about an enzyme?
$K_m$ equals the substrate concentration at half-maximal velocity and inversely reflects affinity: a low $K_m$ means high affinity for the substrate, a high $K_m$ means low affinity.
Give the Lineweaver–Burk (double-reciprocal) equation.
$$\frac{1}{v_0} = \frac{K_m}{V_{max}}\cdot\frac{1}{[S]} + \frac{1}{V_{max}}$$ It linearizes Michaelis–Menten kinetics, with y-intercept $1/V_{max}$ and x-intercept $-1/K_m$.
How do competitive and non-competitive inhibitors differ in their effect on $K_m$ and $V_{max}$?
Competitive inhibitor: increases apparent $K_m$, $V_{max}$ unchanged. Non-competitive inhibitor: $K_m$ unchanged, decreases $V_{max}$.
List the main factors affecting enzyme activity.
Substrate concentration, enzyme concentration, temperature, pH, and presence of activators or inhibitors (including cofactors).
How do temperature and pH affect enzyme activity?
Activity rises with temperature up to an optimum, then falls sharply as the enzyme denatures. Each enzyme has an optimum pH (e.g., pepsin ~2, trypsin ~8); deviations reduce activity by altering ionization/structure.
Classify carbohydrates into their three main groups with examples.
Monosaccharides (glucose, fructose), disaccharides (sucrose, lactose, maltose), and polysaccharides (starch, glycogen, cellulose).
What is the difference between glycolysis's location and its net ATP yield?
Glycolysis occurs in the cytoplasm and converts glucose to 2 pyruvate, with a net gain of 2 ATP and 2 NADH per glucose molecule.
Write the overall net reaction of glycolysis.
$$\ce{Glucose + 2 NAD^+ + 2 ADP + 2 P_i -> 2 Pyruvate + 2 NADH + 2 H^+ + 2 ATP + 2 H2O}$$
What is gluconeogenesis and where does it occur?
Gluconeogenesis is the synthesis of glucose from non-carbohydrate precursors (lactate, glycerol, glucogenic amino acids); it occurs mainly in the liver (and kidney) cytoplasm and mitochondria.
How is glycolysis regulated, naming the key regulatory enzyme?
Regulated at three irreversible steps; the main control point is phosphofructokinase-1 (PFK-1), which is activated by AMP and fructose-2,6-bisphosphate and inhibited by ATP and citrate.
What are the two hormones that reciprocally regulate blood glucose, and their effects?
Insulin lowers blood glucose (promotes glucose uptake, glycogenesis, glycolysis); glucagon raises blood glucose (stimulates glycogenolysis and gluconeogenesis).
Classify lipids into their major categories.
Simple lipids (fats/oils, waxes), compound lipids (phospholipids, glycolipids, lipoproteins), and derived lipids (fatty acids, steroids, cholesterol, ketone bodies).
Where does β-oxidation of fatty acids occur and what does each cycle produce?
In the mitochondrial matrix; each round shortens the fatty acyl chain by 2 carbons and yields 1 acetyl-CoA, 1 FADH2, and 1 NADH.
What is the role of carnitine in fatty acid metabolism?
Carnitine shuttles long-chain fatty acyl groups across the inner mitochondrial membrane (via the carnitine shuttle) so they can undergo β-oxidation in the matrix.
Name the three ketone bodies and the clinical condition of their excess.
Acetoacetate, β-hydroxybutyrate, and acetone; their excess causes ketoacidosis, notably diabetic ketoacidosis.
What is the rate-limiting enzyme of cholesterol synthesis and its target by statins?
HMG-CoA reductase; statins competitively inhibit it, lowering cholesterol synthesis.
Clinically, what does an elevated LDL versus HDL indicate for cardiovascular risk?
High LDL ("bad" cholesterol) deposits cholesterol in arteries and raises atherosclerosis/CVD risk; high HDL ("good" cholesterol) removes cholesterol (reverse transport) and is protective.
What is the structure of DNA according to the Watson–Crick model?
A right-handed antiparallel double helix of two polynucleotide strands, with a sugar-phosphate backbone outside and complementary base pairs (A–T, G–C) hydrogen-bonded inside; ~10 base pairs per turn.
State Chargaff's rules for base composition in DNA.
In double-stranded DNA, the amount of adenine equals thymine ($A = T$) and guanine equals cytosine ($G = C$); thus purines equal pyrimidines ($A+G = T+C$).
How many hydrogen bonds form between A–T and G–C base pairs?
Adenine–Thymine form 2 hydrogen bonds; Guanine–Cytosine form 3 hydrogen bonds (making G–C pairs more stable).
Compare the structural differences between DNA and RNA.
DNA: deoxyribose sugar, thymine base, usually double-stranded, stable. RNA: ribose sugar (2'-OH), uracil instead of thymine, usually single-stranded, less stable.
Name the three main types of RNA and their functions.
mRNA carries the genetic code from DNA to ribosomes; tRNA delivers amino acids matching codons; rRNA forms the structural and catalytic core of the ribosome.
Define the central dogma of molecular biology.
The flow of genetic information: DNA is replicated and transcribed into RNA, which is translated into protein ($\ce{DNA -> RNA -> Protein}$).
What is the difference between transcription and translation?
Transcription synthesizes RNA from a DNA template (in the nucleus, by RNA polymerase); translation synthesizes protein from an mRNA template (on ribosomes, using tRNA).
How is gene expression regulated in prokaryotes via the lac operon?
The lac operon is transcribed only when lactose is present and glucose is low: lactose (allolactose) inactivates the repressor, and low glucose raises cAMP–CAP to activate transcription of lactose-metabolizing genes.
Name the four fat-soluble vitamins and one key function of each.
Vitamin A (vision/epithelial health), Vitamin D (calcium/phosphate homeostasis and bone mineralization), Vitamin E (antioxidant), and Vitamin K (blood clotting factor synthesis).
What deficiency diseases result from lack of vitamins A, D, and K?
Vitamin A deficiency causes night blindness/xerophthalmia; Vitamin D deficiency causes rickets in children and osteomalacia in adults; Vitamin K deficiency causes bleeding disorders (impaired clotting).

Same Biochemistry syllabus in other exams

The Biochemistry outline above is identical in these 2 exams:

Pre-Clinical Biochemistry FAQ

What is in the Pre-Clinical Biochemistry syllabus?

Pre-Clinical Biochemistry is split into 8 chapters: Introduction to Biochemistry, Proteins, Enzymes, Carbohydrates, Lipids, Nucleic Acids, Vitamins and Minerals and Metabolism Integration. Together they contain 23 topics and 75 sub-topics.

How many chapters are in Pre-Clinical Biochemistry?

8 chapters, containing 23 topics and 75 sub-topics. The largest chapter is Proteins, with 3 topics.

Are there flashcards for Pre-Clinical Biochemistry?

Yes — a 51-card Biochemistry deck, printed in full in the flashcards section of this page and available in the Examius app with spaced repetition. The free plan covers one exam of your choice, including its flashcards; Examius Pro, a one-time purchase, unlocks every other exam and deck.