BDS 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 BDS, 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 BDS

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

1. What is the definition and scope of biochemistry?

   Biochemistry is the study of the chemical substances and vital processes occurring in living organisms. Its scope covers the structure, function, and metabolism of biomolecules (carbohydrates, lipids, proteins, nucleic acids), enzymology, molecular genetics, and the chemical basis of health and disease.

2. Why is biochemistry important in dentistry/medicine (BDS)?

   It explains normal metabolic processes, the molecular basis of diseases (e.g., diabetes, caries, osteoporosis), the biochemical basis of drug action, nutrition and vitamin deficiencies, and provides the foundation for interpreting diagnostic lab tests.

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

   Carbohydrates, lipids, proteins, and nucleic acids.

4. Which two organelles are known as the 'powerhouse' and the 'suicidal bags' of the cell?

   The mitochondrion is the powerhouse (site of ATP production via oxidative phosphorylation); the lysosome is the suicidal bag (contains hydrolytic enzymes for intracellular digestion).

5. What are the main functions of the rough and smooth endoplasmic reticulum?

   Rough ER (studded with ribosomes) synthesizes and processes secretory/membrane proteins; smooth ER synthesizes lipids and steroids, detoxifies drugs, and stores $\ce{Ca^2+}$.

6. According to the fluid-mosaic model, what is the basic structure of the plasma membrane?

   A phospholipid bilayer with hydrophilic heads facing outward and hydrophobic tails inward, with proteins (integral and peripheral) floating in a fluid, mosaic-like arrangement; cholesterol modulates fluidity.

7. What is the function of the Golgi apparatus?

   Post-translational modification (e.g., glycosylation), sorting, packaging, and secretion of proteins and lipids received from the endoplasmic reticulum.

8. What is the general structure of an amino acid?

   A central $\alpha$-carbon bonded to an amino group ($\ce{-NH2}$), a carboxyl group ($\ce{-COOH}$), a hydrogen atom, and a variable side chain (R group) that determines the amino acid's properties.

9. How many standard amino acids are there, and how many are essential in humans?

   There are 20 standard amino acids. Nine are essential (must be obtained from diet): histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

10. What is the isoelectric point (pI) of an amino acid?

    The pH at which the amino acid carries no net electrical charge (exists as a zwitterion) and does not migrate in an electric field. For a simple amino acid, $pI = \frac{pK_1 + pK_2}{2}$.

11. Classify amino acids based on side-chain polarity.

    Nonpolar/hydrophobic (e.g., alanine, valine, leucine); polar uncharged (e.g., serine, threonine, glutamine); acidic/negatively charged (aspartate, glutamate); basic/positively charged (lysine, arginine, histidine).

12. What is a zwitterion?

    A dipolar ion carrying both a positive ($\ce{-NH3^+}$) and a negative ($\ce{-COO^-}$) charge simultaneously, giving a net charge of zero; the form in which amino acids exist near neutral pH.

13. Define the four levels of protein structure.

    Primary: linear sequence of amino acids joined by peptide bonds. Secondary: local folding ($\alpha$-helix, $\beta$-pleated sheet) stabilized by hydrogen bonds. Tertiary: overall 3D folding of a single polypeptide. Quaternary: assembly of multiple polypeptide subunits.

14. What type of bond links amino acids in a protein's primary structure?

    The peptide bond, a covalent amide linkage formed between the $\alpha$-carboxyl group of one amino acid and the $\alpha$-amino group of the next, with loss of water (condensation).

15. Which bonds stabilize the secondary structure of proteins?

    Hydrogen bonds between the backbone carbonyl oxygen ($\ce{C=O}$) and amide hydrogen ($\ce{N-H}$) groups; these give rise to the $\alpha$-helix and $\beta$-pleated sheet.

16. List the types of bonds that stabilize tertiary protein structure.

    Hydrophobic interactions, hydrogen bonds, ionic (salt) bridges, van der Waals forces, and covalent disulfide bonds ($\ce{-S-S-}$) between cysteine residues.

17. Give an example of a fibrous and a globular protein with their functions.

    Fibrous: collagen (structural support in connective tissue, bone, dentin). Globular: hemoglobin (oxygen transport) or enzymes (catalysis).

18. What is protein denaturation?

    The disruption of secondary, tertiary, and quaternary structure (without breaking peptide bonds) by heat, pH extremes, or chemicals, leading to loss of biological function; may be reversible or irreversible.

19. How does the structure of hemoglobin relate to its function?

    Hemoglobin is a tetramer ($2\alpha + 2\beta$ subunits), each with a heme group binding one $\ce{O2}$. Cooperative binding (allostery) produces a sigmoidal $\ce{O2}$ dissociation curve, enabling efficient uptake in lungs and release in tissues.

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