MCAT (Medical College Admission Test) Biological and Biochemical Foundations of Living Systems Syllabus

Biological and Biochemical Foundations of Living Systems syllabus — full chapter and topic list

Expand any chapter to see its topics and sub-topics. This is the whole examinable outline for Biological and Biochemical Foundations of Living Systems in MCAT (Medical College Admission Test), not a summary of it.

1. 1

   Biomolecules: Structure and Function

   4 topics

   • Amino Acids and Proteins
     • Classification, side chains, and isoelectric point
     • Primary, secondary, tertiary, and quaternary structure
     • Protein folding, denaturation, and the peptide bond
   • Carbohydrates
     • Monosaccharides, stereochemistry, and anomers
     • Glycosidic linkages and polysaccharides
   • Lipids
     • Fatty acids, triacylglycerols, and phospholipids
     • Steroids, terpenes, and membrane lipids
   • Nucleic Acids
     • Nucleotide structure and base pairing
     • DNA and RNA architecture
2. 2

   Enzymes and Metabolism

   5 topics

   • Enzyme Function and Regulation
     • Active site, specificity, and catalytic mechanisms
     • Michaelis-Menten and Lineweaver-Burk kinetics
     • Competitive, noncompetitive, and allosteric inhibition
   • Carbohydrate Metabolism
     • Glycolysis and gluconeogenesis
     • Citric acid cycle
     • Glycogenesis and glycogenolysis
   • Oxidative Phosphorylation
     • Electron transport chain
     • Chemiosmosis and ATP synthase
   • Lipid and Amino Acid Metabolism
     • Beta-oxidation and ketone bodies
     • Fatty acid synthesis
     • Transamination and the urea cycle
   • Metabolic Integration and Regulation
     • Hormonal control of fed and fasted states
     • Tissue-specific metabolism
3. 3

   Molecular Biology and Genetics

   5 topics

   • DNA Replication and Repair
     • Replication machinery and fidelity
     • Mutations and DNA repair mechanisms
   • Transcription and Translation
     • RNA synthesis and processing
     • The genetic code and ribosomal translation
     • Post-translational modification
   • Gene Expression and Regulation
     • Operons in prokaryotes
     • Eukaryotic transcription factors and epigenetics
   • Classical and Molecular Genetics
     • Mendelian inheritance and pedigrees
     • Linkage, recombination, and Hardy-Weinberg equilibrium
   • Biotechnology Techniques
     • PCR, gel electrophoresis, and cloning
     • DNA sequencing and CRISPR
4. 4

   Cell Biology and Microbiology

   3 topics

   • Cell Structure and Organelles
     • Plasma membrane and transport mechanisms
     • Nucleus, ER, Golgi, and lysosomes
     • Mitochondria and the cytoskeleton
   • The Cell Cycle and Cell Death
     • Mitosis, meiosis, and checkpoints
     • Apoptosis and cancer biology
   • Microbiology and Viruses
     • Prokaryotic structure and reproduction
     • Viral life cycles (lytic and lysogenic)
     • Fungi and bacterial genetics
5. 5

   Human Physiology and Organ Systems

   5 topics

   • Nervous and Endocrine Systems
     • Neuron structure and action potentials
     • Synaptic transmission and reflex arcs
     • Hormonal signaling and feedback loops
   • Circulatory, Respiratory, and Immune Systems
     • Heart anatomy and the cardiac cycle
     • Gas exchange and respiratory mechanics
     • Innate and adaptive immunity
   • Digestive and Excretory Systems
     • Digestion, absorption, and accessory organs
     • Nephron function and osmoregulation
   • Musculoskeletal and Integumentary Systems
     • Muscle contraction and sliding filament theory
     • Bone structure and remodeling
   • Reproduction and Development
     • Gametogenesis and fertilization
     • Embryonic development and differentiation

Biological and Biochemical Foundations of Living Systems flashcards for MCAT (Medical College Admission Test)

21 of 51 cards from the Biological and Biochemical Foundations of Living Systems deck — real questions with worked answers.

1. What distinguishes the structures of the 20 standard amino acids from one another?

   Their R-group (side chain), which determines polarity, charge, and chemical behavior. All share a central alpha carbon bonded to an amino group, a carboxyl group, and an H.

2. Name the only achiral standard amino acid and explain why.

   Glycine, because its R-group is a single hydrogen atom, so the alpha carbon has two identical H substituents and is not a stereocenter.

3. What four levels of protein structure exist, and what stabilizes each?

   Primary (peptide bonds), secondary (H-bonds in backbone forming alpha-helices/beta-sheets), tertiary (R-group interactions: disulfide bonds, hydrophobic, ionic, H-bonds), quaternary (interactions between multiple subunits).

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

   The pH at which the molecule carries no net charge (exists as a zwitterion). For a simple amino acid, pI = average of the two relevant pKa values.

5. What is the general molecular formula of carbohydrates, and how are monosaccharides classified?

   (CH2O)n. Classified by number of carbons (triose, pentose, hexose) and by carbonyl type: aldoses (aldehyde) or ketoses (ketone).

6. Distinguish alpha and beta anomers of a cyclic sugar.

   They differ in configuration at the anomeric carbon: in alpha the OH is on the opposite side (axial/trans) from the CH2OH reference; in beta it is on the same side (cis). E.g., alpha-glucose vs beta-glucose.

7. Compare the glycosidic linkages in starch, glycogen, and cellulose.

   Starch and glycogen use alpha-1,4 linkages (with alpha-1,6 branches); cellulose uses beta-1,4 linkages, making it indigestible to humans and structurally rigid.

8. What functional definition distinguishes lipids from other macromolecules?

   Lipids are defined by solubility, not structure: they are hydrophobic/amphipathic molecules soluble in nonpolar solvents but insoluble in water.

9. What is the difference between saturated and unsaturated fatty acids?

   Saturated fatty acids have no C=C double bonds (straight chains, solid at room temp); unsaturated have one or more double bonds (kinks, lower melting point, often liquid).

10. Describe the structure of a phospholipid and why it forms bilayers.

    A glycerol backbone with two hydrophobic fatty acid tails and a hydrophilic phosphate head. This amphipathic nature drives spontaneous bilayer formation in water.

11. What are the components of a nucleotide?

    A five-carbon sugar (ribose or deoxyribose), a nitrogenous base, and one to three phosphate groups.

12. State Chargaff's rules and the base-pairing scheme of DNA.

    In DNA, A pairs with T (2 H-bonds) and G pairs with C (3 H-bonds); thus %A=%T and %G=%C. Purines (A, G) pair with pyrimidines (C, T).

13. How do the strands of a DNA double helix run relative to one another?

    Antiparallel: one strand runs 5' to 3' while the complementary strand runs 3' to 5'.

14. What is the difference between competitive and noncompetitive enzyme inhibition (effect on Km and Vmax)?

    Competitive: inhibitor binds active site; raises apparent Km, Vmax unchanged. Noncompetitive: binds allosteric site; Vmax decreases, Km unchanged.

15. What does the Michaelis constant (Km) represent?

    The substrate concentration at which reaction velocity is half of Vmax. A low Km indicates high enzyme affinity for the substrate.

16. What is feedback inhibition in metabolic regulation?

    The end product of a pathway allosterically inhibits an enzyme earlier in the pathway (often the committed/rate-limiting step), preventing overaccumulation.

17. What are the net products of glycolysis per glucose molecule?

    2 pyruvate, 2 net ATP, and 2 NADH. Glycolysis occurs in the cytoplasm.

18. What is the rate-limiting enzyme of glycolysis and how is it regulated?

    Phosphofructokinase-1 (PFK-1). It is inhibited by ATP and citrate and activated by AMP and fructose-2,6-bisphosphate.

19. What are the per-turn products of the citric acid (Krebs) cycle?

    Per acetyl-CoA: 3 NADH, 1 FADH2, 1 GTP (or ATP), and 2 CO2. It occurs in the mitochondrial matrix.

20. What is the role of the electron transport chain and the final electron acceptor?

    It uses NADH and FADH2 to pump protons across the inner mitochondrial membrane, creating a gradient. Oxygen is the final electron acceptor, forming water.

21. How does ATP synthase produce ATP (chemiosmosis)?

    Protons flow down their electrochemical gradient through ATP synthase from the intermembrane space into the matrix; this flow drives phosphorylation of ADP to ATP.

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