University of St Andrews

Key information

SCOTCAT credits : 20

ECTS credits : 10

Level : SCQF level 9

Semester: 1

Availability restrictions: Not capped

Planned timetable: 9.00 am Mon, Tue & Wed (Lectures); 9.00 am Thu & Fri (Practicals)

This module covers advanced aspects of protein science. The module introduces the major techniques for protein structure determination that are at the heart of biochemistry, molecular biology and drug discovery. The physical principles behind and strategies for elucidating protein structures by X-ray crystallography, NMR spectroscopy and cryo-electron microscopy are discussed. Membrane proteins are considered as an example of the impact of structural information on understanding biological function. The second part builds an understanding of thermodynamic and kinetic principles of protein interactions. Protein engineering by directed evolution will be introduced. This section is complemented by advanced aspects of enzyme kinetics and enzyme inhibition. The third part of the module considers protein folding and misfolding. It will be examined how proteins achieve functional three-dimensional structures. Protein misfolding diseases are used as examples to highlight the significance of protein folding. Prions and the molecular basis of spongiform encephalopathies are discussed in detail.

Relationship to other modules

Pre-requisite(s): Before taking this module you must pass BL2306 and ( pass BL2302 or pass BL2309 )

Learning and teaching methods and delivery

Weekly contact: Across the semester: 29 x 1h lectures, 4 x 1h tutorials, 2 x 8h practicals split over several days

Scheduled learning hours: 51

Guided independent study hours: 140

Assessment pattern

As used by St Andrews: 3-hour Written Examination = 50%, Coursework = 50%

As defined by QAA
Written examinations : 50%
Practical examinations : 0%
Coursework: 50%

Re-assessment: 3-hour Written Examination = 50%, Coursework = 50%

Personnel

Module coordinator: Dr U Schwarz-Linek
Module teaching staff: Team taught