Proteins and Macromolecular Assemblies
Life Sciences (School of)
Undergraduate: Level 5
Thursday 03 October 2019
Saturday 14 December 2019
05 September 2019
Requisites for this module
BSC C700 Biochemistry,
BSC C701 Biochemistry (Including Placement Year),
BSC C703 Biochemistry (Including Year Abroad),
BSC CR00 Biochemistry (Including Foundation Year)
Proteins have a central role in many of life's essential processes. Often proteins do not act alone, but in tandem with a partner protein or other biological molecules such as DNA, RNA or a lipid. These interactions can lead to the formation of larger macromolecular assemblies, often termed molecular machines, which are involved in cell processes ranging from biological protein synthesis (translation) to initiating apoptosis (cell death).
Methods and techniques that enable a protein or enzyme to be biochemically and structurally characterised will be introduced and methods to study protein folding, protein-protein interactions and structure/function studies of selected macromolecular assemblies will be addressed.
The aim of this module is to build on the basic principles of protein structure and function obtained from BS131.
To pass this module students will need to be able to:
1. discuss methods to obtain pure proteins and protein assemblies;
2. understand the key factors that influence protein folding and putative mechanisms that explain the time course of this process and techniques used to study folding;
3. describe steady-state enzyme kinetics, analysis of enzyme inhibition and methods to determine the mechanism of action of an enzyme;
4. describe techniques used to study binding of proteins to partners and the thermodynamic and kinetic parameters that may be obtained;
5. understand protein structure-function relationships and have an overview of structural biology techniques available, particularly X-ray crystallography;
6. understand the analysis and prediction of protein structures;
7. discuss examples of macromolecular assemblies, their function, how they are assembled and techniques other than X-ray crystallography that can be used to study their structure.
No additional information available.
18 x 1 hour lectures, plus 1 revision class before summer exam; 2 x 3 hour practical
- Serdyuk, Igor N.; Zaccai, Nathan R.; Zaccai, G. (2007) Methods in molecular biophysics: structure, dynamics, function, Cambridge: Cambridge University Press.
- Rupp, Bernhard. (c2010) Biomolecular crystallography: principles, practice, and application to structural biology, New York: Garland Science.
The above list is indicative of the essential reading for the course. The library makes provision for all reading list items, with digital provision where possible, and these resources are shared between students. Further reading can be obtained from this module's reading list.
Assessment items, weightings and deadlines
|Coursework / exam
||120 minutes during Summer (Main Period) (Main)
Module supervisor and teaching staff
Dr Jonathan Worrall, email: email@example.com.
Dr Jonathan Worrall, Dr Mike Hough
School Undergraduate Office, email: bsugoffice (Non essex users should add @essex.ac.uk to create the full email address)
Dr Clive Butler
The University of Exeter
Associate Professor of Microbial Biochemistry
Available via Moodle
Of 49 hours, 19 (38.8%) hours available to students:
30 hours not recorded due to service coverage or fault;
0 hours not recorded due to opt-out by lecturer(s).
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