Introductory Biochemistry
The molecules of life and the chemistry that connects them: the elements, functional groups and weak interactions of biomolecules; water, the hydrophobic effect, pH, the Henderson–Hasselbalch equation and the buffers of the blood; amino acids, their charges and isoelectric points, and the planar peptide bond; the four levels of protein structure, folding, denaturation and misfolding, and cooperative oxygen binding by hemoglobin; enzyme catalysis, Michaelis–Menten kinetics, inhibition and allosteric regulation; monosaccharides, ring forms, glycosidic bonds, starch, glycogen and cellulose; fatty acids, fats, membrane lipids, the fluid mosaic model and membrane transport; nucleotides, the double helix, RNA and the flow of genetic information; free energy, coupling by ATP and redox carriers; glycolysis and its control; pyruvate dehydrogenase, the citric acid cycle, the respiratory chain and chemiosmotic ATP synthesis; and a capstone on beta-oxidation, ketone bodies, amino acid breakdown, gluconeogenesis and the hormonal integration of metabolism, with runnable Python programs throughout.
BIOC-200 Year 2 3 credits 12 lessons · 4 h 57 min ▶ Video lessons coming soon
Offered by HSM University · Biochemistry
This is the American version of this course. See the Canadian version.
What you'll learn
- Describe the elements, functional groups, linkages and weak interactions of biological molecules, and explain how monomers build the four classes of macromolecules.
- Explain the properties of water and the hydrophobic effect, calculate pH, and use the Henderson–Hasselbalch equation to design buffers and interpret the bicarbonate buffer of blood.
- Describe the structure and ionization of amino acids, classify the twenty side chains, calculate the net charge and isoelectric point of peptides, and explain the planar peptide bond.
- Describe the four levels of protein structure and the forces that stabilize them, explain folding, denaturation and misfolding, and relate the structures of myoglobin and hemoglobin to cooperative oxygen binding.
- Explain how enzymes lower activation energies, analyze rates with the Michaelis–Menten equation, kcat and kcat/KM, distinguish types of inhibition, and describe how enzymes are regulated.
- Classify monosaccharides, describe ring formation and anomers, and relate the glycosidic bonds of disaccharides and polysaccharides to their roles in energy storage, structure and recognition.
- Describe fatty acids, triacylglycerols, phospholipids and sterols, explain the structure and fluidity of membranes, and calculate the free energy of ion gradients that drive transport.
- Describe nucleotides and the double helix, apply base-pairing rules and Chargaff's rules, explain melting and hybridization, compare DNA and RNA, and outline the flow of genetic information.
- Apply ΔG = ΔG°′ + RT ln Q and ΔG°′ = −RT ln K, explain coupling by ATP, calculate free energies from reduction potentials, and distinguish catabolism from anabolism.
- Trace the ten steps of glycolysis, account for its ATP and NADH, explain its control at phosphofructokinase-1 and the other irreversible steps, and describe the fates of pyruvate.
- Describe pyruvate dehydrogenase, the citric acid cycle and the respiratory chain, explain chemiosmotic ATP synthesis and uncoupling, and calculate the ATP yield of glucose oxidation.
- Outline beta-oxidation, ketone bodies, amino acid breakdown and the urea cycle, gluconeogenesis and fuel storage, and explain how insulin and glucagon coordinate the organs in the fed and fasting states.
Course content
12 lessons · 4 h 57 min total · final exam
- 1 Biochemistry: the chemistry of living things 26 min · quiz
- 2 Water, pH and buffers 26 min · quiz
- 3 Amino acids and the peptide bond 27 min · quiz
- 4 Protein structure and function 25 min · quiz
- 5 Enzymes: how biological catalysts work 25 min · quiz
- 6 Carbohydrates 23 min · quiz
- 7 Lipids and biological membranes 25 min · quiz
- 8 Nucleic acids 24 min · quiz
- 9 Bioenergetics and ATP 24 min · quiz
- 10 Glycolysis 24 min · quiz
- 11 The citric acid cycle and oxidative phosphorylation 24 min · quiz
- 12 Capstone: fats, amino acids and the integration of metabolism 24 min · quiz
- E Final exam 20 questions
Requirements
Recommended background. You can start any course at any time.
Description
The molecules of life and the chemistry that connects them: the elements, functional groups and weak interactions of biomolecules; water, the hydrophobic effect, pH, the Henderson–Hasselbalch equation and the buffers of the blood; amino acids, their charges and isoelectric points, and the planar peptide bond; the four levels of protein structure, folding, denaturation and misfolding, and cooperative oxygen binding by hemoglobin; enzyme catalysis, Michaelis–Menten kinetics, inhibition and allosteric regulation; monosaccharides, ring forms, glycosidic bonds, starch, glycogen and cellulose; fatty acids, fats, membrane lipids, the fluid mosaic model and membrane transport; nucleotides, the double helix, RNA and the flow of genetic information; free energy, coupling by ATP and redox carriers; glycolysis and its control; pyruvate dehydrogenase, the citric acid cycle, the respiratory chain and chemiosmotic ATP synthesis; and a capstone on beta-oxidation, ketone bodies, amino acid breakdown, gluconeogenesis and the hormonal integration of metabolism, with runnable Python programs throughout.
Part of the Science stream, typically taken in year 2.