Target Students:  Compulsory for all students registered for single honours degrees in Biochemistry with ‘without another subject and other qualified students, approved by the Head of Biochemistry. There is a limited number of places on this module. Students are reminded that enrolments which are not agreed by the Offering School in advance may be cancelled without notice.

Taught Semesters:

Prerequisites: 

Corequisites:  None.

Summary of Content:  The structure and function of soluble proteins; how individual proteins can be studied in molecular detail; the problems associated with studying membrane-bound proteins; enzyme kinetics and catalysis; practical aspects of affinity purification, SDS PAGE, western blotting, enzyme assays, bioinformatics and molecular modelling approaches. Module Web Links:

Method and Frequency of Class:
Specific Activities are not listed
Further Activity Details:
2 lecture sessions per week, 7 practical sessions at weekly intervals >weeks 1; all students >weeks 2-7; students in two parallel groups Activities include lectures, practicals and workshops. Please refer to the module timetable online for up to date information on contact hours

Method of Assessment: 

Convenor: 
Dr R Layfield
Dr C Friel

Education Aims:  Students will be able to describe the general structure of soluble proteins; they will learn about methods to analyse the different levels of protein structure; they will gain knowledge about the specific properties of structural and myofibrillar proteins; they will be able to describe the structure of several specific membrane-bound proteins and the challenges associated with their purification; they will know how enzymes operate in mono and bi-substrate reactions and be able to describe the kinetics of such enzyme-catalysed reactions; they will be able to discuss complex enzyme mechanisms and how these enzyme actions are controlled; they will learn about methodologies to study protein interactions and the research applications of proteins; they will explore the concept of orchestrated interaction of protein in vivo (both transient and stable). They will support theoretical knowledge with practical experience of different analytical approaches required to study and purify proteins and enzymes, and hands-on bioinformatics analyses of protein sequence data.