Pre-Clinical Biochemistry Syllabus

Biochemistry syllabus — full chapter and topic list

Expand any chapter to see its topics and sub-topics. This is the whole examinable outline for Biochemistry in Pre-Clinical, not a summary of it.

1. 1

   Introduction to Biochemistry

   2 topics

   • Scope and Importance
     • Definition of Biochemistry
     • Applications in Medicine
     • Historical Development
   • Cell Structure and Functions
     • Cell Membrane
     • Organelles
     • Cytoskeleton
2. 2

   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
3. 3

   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
4. 4

   Carbohydrates

   3 topics

   • Classification
     • Monosaccharides
     • Disaccharides
     • Oligosaccharides
     • Polysaccharides
   • Metabolism
     • Glycolysis
     • Gluconeogenesis
     • Glycogen Metabolism
     • Pentose Phosphate Pathway
   • Regulation
     • Hormonal Regulation
     • Allosteric Regulation
5. 5

   Lipids

   3 topics

   • Classification
     • Fatty Acids
     • Triglycerides
     • Phospholipids
     • Steroids
   • Metabolism
     • Beta-Oxidation
     • Fatty Acid Synthesis
     • Cholesterol Metabolism
     • Lipoprotein Metabolism
   • Clinical Aspects
     • Hyperlipidemia
     • Atherosclerosis
     • Obesity
6. 6

   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
7. 7

   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
8. 8

   Metabolism Integration

   3 topics

   • Energy Balance
     • ATP
     • Energy Yield of Macronutrients
   • Metabolic Pathways
     • Catabolic Pathways
     • Anabolic Pathways
   • Hormonal Regulation
     • Insulin
     • Glucagon
     • Thyroid Hormones

Biochemistry flashcards for Pre-Clinical

19 of 51 cards from the Biochemistry deck — real questions with worked answers.

1. 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.

2. List the four major classes of biomolecules studied in biochemistry.

   Carbohydrates, lipids, proteins, and nucleic acids.

3. 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.

4. 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.

5. 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.

6. 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.

7. 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.

8. 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.

9. 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: $$pI = \frac{pK_{a1} + pK_{a2}}{2}$$

10. 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).

11. 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).

12. 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.

13. 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.

14. 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.

15. 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).

16. 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.

17. 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).

18. 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).

19. 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.

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