Biochemistry

BIOC 222: Proteins and Biotechnology

In this course we introduce students to the fundamental properties of proteins, with a focus on how ‘sequence determines structure’ and ‘structure determines function’.  We also explore the mechanisms by which cells control and modify protein function.  We examine how a protein’s lifetime is regulated and how a protein’s activity can be stimulated or repressed by different modifications.

The basic properties of enzymes are introduced and we study specific examples of catalysis.  How proteins and enzymes can be engineered, and the industrial application of enzymes and their use as drug targets are also be studied.  Common techniques used to study proteins are reviewed.  The course concludes by bringing together this knowledge using examples of specific new biotechnological processes and how these will influence medicine, agriculture and biodiversity.

The project-based, modular laboratory course reinforces the lecture material and provides hands on experience in molecular biology research.

Protein Structure and Function (11 lectures)

Protein biochemistry: amino acids and proteins. Protein structure and folding – primary, secondary, tertiary and quarternary. Enzymes – active sites and recognition. Enzyme kinetics, influence of temperature and pH. Examples of catalysis.


Control of Protein Function (9 lectures)

Control of enzyme activity, including concepts of allostery and cooperativity, covalent modification, modulation by ligands and ATP hydrolysis.  Measurement of protein activation and binding.  Mechanisms of protein localisation and turnover, including signal sequences, translocation machinery, ubiquitination and directed degradation.

Protein Biotechnology (10 lectures)   

Protein purification: chromatography based on chemistry, size and activity. Analysis of concentration and purity. Recombinant protein expression – advantages/disadvantages.
Mutagenesis and protein engineering. Proteins as drug targets and the rational design of proteins.