The main aim of the module is to equip the students with fundamental principles of theory and practical aspects of protein science that investigates the intricate relationship between biomolecular structure and function and enzymology. The material is presented at a level suitable for students from any Molecualr Biosciences programme, and to a depth appropriate both for the students who will not continue to study in the subject area and those who will progress to advanced (third year) protein structure/function courses. The learning objectives of the module are addressed within lectures and small group tutorials in the first term, and workshops and practical sessions in the second term.

Building on the knowledge acquired in the first year, after taking this module you will be able to:

Understand the basis of the mechanisms, thermodynamics and kinetics of protein folding and the nature of the forces which maintain the native state.
	Consider protein mutations in a context of protein folding diseases.
	Understand the role of higher orders of structure, including secondary, super-secondary and domain structures.
	Appreciate the physical and chemical methods used in the determination of three-dimensional protein structure.
	Understand the principles, practice and problems associated with heterologous protein expression and separation and be aware of the high-throughput methods used in protein production and analysis.
	Understand the principles of simple one and two-substrate enzyme reaction kinetics and determine experimentally the basic kinetic constants for an enzyme reaction.
	Understand the importance of co-enzymes and cofactors in enzyme reaction mechanisms.
	Analyse enzyme reaction mechanisms using the range of structural and functional data.
	Understand the structures and functional roles of number of proteins, in particular haemoglobin, DNA polymerase, proteins in bacterial pilus biogenesis, antibodies, and membrane proteins.
	Become aware of the significance of binding equilibrium and its implications for ligand/receptor and substrate/enzyme reactions
	To consider protein stability and understand the importance of thermodynamic, thermal and chemical stability.
	To understand the relationship between Gibbs free energy and protein stability as well as various factors that impact protein stability.
Indicative lecture list (based on 2021/22)

Protein Structure principles
	Classification of protein folds
	Protein energetic and dynamics
	Protein folding/intra- and inter molecular forces
	Protein purification methods/high throughput
	Protein characterisation (X-ray crystallography/NMR/EM/binding equilibrium)
	Protein/DNA interaction: DNAP
	Pilus biogenesis
	Myoglobin and haemoglobin
	Membrane proteins
	GPCRs and heterologous protein expression
	Energetics of protein stability
	Factors impacting protein stability
	Ribosomes
	Antibodies
	Fundamental principles of enzyme kinetics
	The specificity constant and two-substrate mechanisms
	Inhibition of enzyme-catalysed reactions
	Enzymes: effect of pH; recognising cooperativity
	Catalytic strategies
	Enzyme mechanisms