Most biological processes involve interactions between macromolecules. The module discusses selected examples and explains techniques used to study molecular interactions.
PRE-REQUISITES BIOL2010 and either of (BIOL2011 or BIOL2012)
Aims and Objectives
Having successfully completed this module you will be able to:
- describe protein ligand interactions;
- regulation of kinase activity;
- describe the structure of DNA and the nature of interactions with proteins;
- describe hydrogen–deuterium exchange in mass spectrometry to study molecular interaction.
- describe the structure of RNA and the nature of riboswitches;
- multi-domain proteins, their structure and function;
- describe GTPases as molecular protein switches;
- describe how peptide motifs are recognised by interacting proteins;
The module discusses ways in which signal transduction events lead to altered gene expression. Cytokines and growth hormones and their receptors are discussed, affecting cell cycle regulation. Protein-peptide recognition will be introduced, and will see how viruses upset cell regulation through interfering peptides. The receptors themselves are often multi-domain proteins. Assembly of multiple domains is a requirement for regulation and efficient binding site presentation. The structure of DNA and the recognition of nucleic acids by interacting proteins such as histones, nucleases, and transcription factors is introduced. Also discussed are the structures of RNA and riboswitches. Methods to study macromolecular interactions are introduced in all sections. The seminal technique of mass spectrometry is covered in detail to explain protein-ligand interactions. Hydrogen–deuterium exchange (HDX) mass spectrometry allows to studying protein-protein interactions.
Learning and Teaching
Teaching and learning methods
Lectures and independent study.
|Total study time||150|
This is how we’ll formally assess what you have learned in this module.
This is how we’ll assess you if you don’t meet the criteria to pass this module.