BL3301 Protein Structure and Function

Academic year

2024 to 2025 Semester 1

Further information on which modules are specific to your programme.

Key module information

SCOTCAT credits

20

The Scottish Credit Accumulation and Transfer (SCOTCAT) system allows credits gained in Scotland to be transferred between institutions. The number of credits associated with a module gives an indication of the amount of learning effort required by the learner. European Credit Transfer System (ECTS) credits are half the value of SCOTCAT credits.

SCQF level

SCQF level 9

The Scottish Credit and Qualifications Framework (SCQF) provides an indication of the complexity of award qualifications and associated learning and operates on an ascending numeric scale from Levels 1-12 with SCQF Level 10 equating to a Scottish undergraduate Honours degree.

Availability restrictions

Not capped

Planned timetable

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

This information is given as indicative. Timetable may change at short notice depending on room availability.

Module coordinator

Dr U Schwarz-Linek

This information is given as indicative. Staff involved in a module may change at short notice depending on availability and circumstances.

Module Staff

Team taught

This information is given as indicative. Staff involved in a module may change at short notice depending on availability and circumstances.

Module description

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-requisites

BEFORE TAKING THIS MODULE YOU MUST PASS BL2306 AND ( PASS BL2302 OR PASS BL2309 )

Assessment pattern

Written Examination = 50%, Coursework = 50%

Re-assessment

3-hour Written Examination = 50%, Coursework = 50%

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

The number of compulsory student:staff contact hours over the period of the module.

Guided independent study hours

140

The number of hours that students are expected to invest in independent study over the period of the module.