Biochemistry

BIOC 192: Foundations of Biochemistry

Biochemistry is ‘the chemistry of life’ , a combination of chemistry and biology, but this definition does not convey properly the breadth and impact of modern biochemistry.  A biochemist is a scientist who uses the languages of chemistry and physics to describe the processes occurring in that self-replicating, self-repairing chemical machine that is the living cell.  Essentially there are four main areas of study:

1. The materials from which cells are made (proteins, lipids, carbohydrates, nucleic acids, etc. – the ‘molecules of life’).
2. The way in which these molecules are made, changed and degraded (metabolism).
3. The sources of energy for synthesis and maintenance (bioenergetics).
4. The storage, transmission and interpretation of genetic information.

BIOC 192 provides an introduction to the first three of these, whereas the fourth area is outlined in CELS 191 and is covered in greater detail in BIOC 221.  In recent years the term molecular biology has been increasingly used by both the scientific and medical communities to emphasise more the genetic aspects of biochemistry, reinforced by the developments in gene technology.  As most genes code for proteins, and most genetic events are controlled by proteins, you can see that biochemistry, molecular biology and genetics overlap to a large degree.

From early last century, biochemistry has had a close association with human medicine.  Most departments of biochemistry were established in medical schools, as it became abundantly clear that human physiology needed to be studied at the molecular level.  Biochemistry has strong links with almost every branch of the biological and medical sciences.  The term molecular medicine is now widely used to convey our increasing knowledge of the molecular basis of disease.  In BIOC 192 you will be introduced to this pool of knowledge by learning some of the fundamental concepts of biochemistry with reference to health and disease.

Lectures:

1. Introduction to proteins
2. Elements of protein structure #1
3. Elements of protein structure #2
4. Genes to proteins to new medicines
5. Haemoglobin as a model protein #1
6. Haemoglobin as a model protein #2
7. Haemoglobin variants
8. Post-translational modifications
9. Biotechnology: synthesis of pharmaceutical proteins
10. Enzymes - introduction and substrate interactions
11. Enzyme kinetics #1
12. Enzyme kinetics #2
13. Enzyme regulation
14. Applications of enzymes in health sciences
15. Membrane lipids and proteins
16. Membrane channels and transporters
17. Ion Channels as Drug Targets #1
18. Ion Channels as Drug Targets #2
19. G-protein coupled and steroid receptors
20. Energy from food
21. Digestion and absorption of carbohydrates
22. Digestion and absorption of proteins and nucleic acids
23. Digestion and absorption of lipids
24. Lipoproteins and lipid transport pathways
25. The biochemistry of heart disease
26. Vitamins
27. Minerals
28. Overview of metabolism: bioenergetics
29. Acetyl-CoA and the citric acid cycle
30. Electron transport chain
31. Oxidative phosphorylation
32. Fatty acid oxidation
33. Glycolysis
34. Oxidation of amino acids and inborn errors of metabolism
35. Antioxidants and reactive oxygen species
36. Alcohol metabolism
37. Fuel storage and mobilisation
38. Starvation
39. Exercise biochemistry
40. Metabolism in the Antarctic
41. Diabetes
42. Obesity
43. Integration and regulation of metabolism

 

Practical Sessions:

Units, pipetting, and spectrophotometry
Provides the foundation for the laboratory course. Covers: common units and their interconversion;the use of variable volume micropippetors; the theory and practice of spectrophotometry.

Quantitative assay and electrophoresis of serum proteins
Examines two methods for examining complex solutions: specific assay and fractionation. A colorimetric assay of proteins is undertaken and the use of standard curves highlighted. Fractionation of plasma and serum proteins (using both normal and abnormal patient samples) via native gel electrophoresis is undertaken. The principles guiding the safe handling of biological samples are highlighted. Clinical relevance examples are considered.

Enzyme kinetics
This laboratory is designed to highlight the experimental determination of kinetic principles discussed in lectures. Experiments on the relationship between enzyme concentration and catalytic rate, and between substrate concentration and catalytic rate are undertaken. Data collected is used to determine the kinetic parameters of the enzyme under investigation and confirm mathematical expressions outlined in lectures. The content of this laboratory is developed further in a selfdirected learning exercise the students undertake.

Gel permeation chromatography and spectrophotometry of haemoglobin
Haemoglobin derivatives discussed in lectures are generated and analysed spectrophotometrically. Fractionation by gel permeation chromatography is undertaken, using haemoglobin derivatives to trace the progress of the experiment. Clinical relevance examples are considered.

Blood lipoproteins and cholesterol
Student volunteers perform a spectrophotometric assay to determine their plasma cholesterol and examine their plasma liporotein profile by gel electrophoresis. The principles guiding the safe handling of biological samples are highlighted. The use of enzymes to analyse complex solutions is considered, as are examples of clinical relevance.

Enzyme assay of blood glucose and commercial beverages
Student volunteers undertake a modified glucose tolerance test and use a spectrophotometric assay to determine the amount of glucose in a commercial beverage. The principles guiding the safe handling of biological samples are highlighted. The use of enzymes to analyse complex solutions is considered, as are examples of clinical relevance.