Molecular Recognition

Learning Outcomes

Learning Outcomes

Having successfully completed this module you will be able to:

• understand the mechanism and role of cellular glycosylation machinery linked to protein fate
• critically assess how multi-domain proteins regulate physiology through protein-protein interactions
• understand multi-domain proteins, their structure and function
• evaluate how peptide motifs are recognised by interacting proteins
• understand the central role of GTPases as molecular protein switches
• understand how cell signalling through cytokines and growth hormones changes cellular fate
• understand how hydrogen–deuterium exchange in mass spectrometry can be used to study molecular interaction
• critically assess how glycosylation influences molecular interaction

The first section introduces signal transduction events that lead to altered gene expression. Examples such as cytokines and growth hormones and their receptors are discussed. Proteins circulating in the blood and extracellular proteins are typically glycosylated, and the next section will introduce how glycans are edited. Glycans provide altered protein functionality and alter recognition. Examples are glycan mediated protein-protein interactions and immune evasion. Cellular receptors are often multi-domain proteins, as we will see in the next section. Assembly of multiple domains is a requirement for regulation and efficient binding site presentation. The seminal technique of mass spectrometry is covered in the third section to explain protein-ligand interactions. Hydrogen–deuterium exchange (HDX) mass spectrometry allows to studying protein- protein interactions. Methods to study macromolecular interactions are introduced in all sections.

Lectures and independent study. Coursework with feedback to the student.

Summative

This is how we’ll formally assess what you have learned in this module.

Referral

This is how we’ll assess you if you don’t meet the criteria to pass this module.