Proteins: Structure and Function - BIOS6290

Looking for a different module?

Module delivery information

Location Term Level1 Credits (ECTS)2 Current Convenor3 2021 to 2022
Canterbury
Autumn Term 6 30 (15) Richard Williamson checkmark-circle

Overview

The module will cover the structural analysis of proteins and protein assemblies using techniques such as fluorescence, circular dichroism, mass spectrometry, atomic-force microscopy, cryo-EM, X-ray crystallography and NMR. It will also look at protein folding, molecular processing, de novo design, engineering and modelling. The module will also investigate the relationship between protein structure and function and cover the principles and practice of enzymology, ligand binding, and enzyme catalysis.

Details

Contact hours

Total contact hours: 70
Private study hours: 230
Total study hours: 300

Method of assessment

Course work assignments (x3). Handling, analysis and interpretation of experimental data. (13.3% each)
Exam 1 (2h) Essay (30%)
Exam 2 (2h) Problem solving (30%)

Indicative reading

Williamson, M. (2011) How Proteins Work. Garland Science
Lesk, A.M. (2016, 3nd ed.) Introduction to Protein Science. Architecture, function and genomics. Oxford University Press
Price & Nairn (2009) Exploring Proteins. Oxford University Press
Rhodes G (2006, 3rd ed.) Crystallography Made Crystal Clear. Academic Press
Steven, Baumeister, Johnson & Perham (2016) Molecular Biology of Assemblies and Machines.

See the library reading list for this module (Canterbury)

Learning outcomes

The intended subject specific learning outcomes. On successfully completing the module students will be able to:

Demonstrate an understanding of the structural organisation and biophysical properties of proteins together with their physiological function in terms of catalysis, ligand binding and as components of molecular machines.
Demonstrate an understanding of how the structure and function of proteins are studied and characterised using current biophysical methods such as mass spectroscopy, x-ray diffraction, nuclear magnetic resonance, fluorescence, circular dichroism, electron microscopy, atomic force microscopy and rapid mixing apparatus.
Use web-based tools to retrieve and manipulate protein-related data from international repositories, and the use of molecular graphics software to analyse protein structure in relation to topology and function.
Demonstrate knowledge and understanding of the instrumentation and the type of data generated by the techniques listed above using modern research equipment in the Research Facilities and Research Labs of the School of Biosciences.


The intended generic learning outcomes. On successfully completing the module students will be able to:

Communicate effectively using writing.
Handle and analyse experimental data (including numerical data).
Problem solve.
Use web tools, data repositories, and computer software.

Notes

  1. Credit level 6. Higher level module usually taken in Stage 3 of an undergraduate degree.
  2. ECTS credits are recognised throughout the EU and allow you to transfer credit easily from one university to another.
  3. The named convenor is the convenor for the current academic session.
Back to top

University of Kent makes every effort to ensure that module information is accurate for the relevant academic session and to provide educational services as described. However, courses, services and other matters may be subject to change. Please read our full disclaimer.