BIOL3013 Molecular Recognition
Module Overview
Most biological processes involve interactions between macromolecules. It is the aim of this module to illustrate the nature of these interactions with selected examples. The first section introduces the structure of DNA and the recognition of nucleic acids by interacting proteins such as histones, nucleases, and transcription factors. Also discussed are the structure of RNA and riboswitches. From the nucleus of the cell, we turn our attention to the surface of the cell, and discuss ways in which signal transduction events lead to altered gene expression. Examples such as 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, as we will see in the next section. Assembly of multiple domains is a requirement for regulation and efficient binding site presentation. Methods to study macromolecular interactions are introduced in all sections. The seminal technique of mass spectrometry is covered in the final section to explain protein-ligand interactions. Hydrogen–deuterium exchange (HDX) mass spectrometry allows to studying protein-protein interactions.
Aims and Objectives
Learning Outcomes
Learning Outcomes
Having successfully completed this module you will be able to:
- describe the structure of DNA and the nature of interactions with proteins;
- describe the structure of RNA and the nature of riboswitches;
- describe GTPases as molecular protein switches;
- describe how peptide motifs are recognised by interacting proteins;
- describe ligand recognition in the immune system;
- describe protein ligand interactions;
- describe hydrogen–deuterium exchange in mass spectrometry to study molecular interaction.
Syllabus
Most biological processes involve interactions between macromolecules. It is the aim of this module to illustrate the nature of these interactions with selected examples. The first section introduces the structure of DNA and the recognition of nucleic acids by interacting proteins such as histones, nucleases, and transcription factors. Also discussed are the structure of RNA and riboswitches. From the nucleus of the cell, we turn our attention to the surface of the cell, and discuss ways in which signal transduction events lead to altered gene expression. Examples such as 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, as we will see in the next section. Assembly of multiple domains is a requirement for regulation and efficient binding site presentation. Methods to study macromolecular interactions are introduced in all sections. The seminal technique of mass spectrometry is covered in the final section 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 with some informal tutorials.
| Type | Hours |
|---|---|
| Lecture | 24 |
| Independent Study | 126 |
| Total study time | 150 |
Assessment
Summative
| Method | Percentage contribution |
|---|---|
| Written exam (2 hours) | 100% |
Referral
| Method | Percentage contribution |
|---|---|
| Written exam (2 hours) | 100% |
Linked modules
PRE-REQUISITES BIOL2010 AND BIOL2011 OR BIOL2012