BS230-5-AU-CO:
Proteins and Macromolecular Assemblies

The details
2019/20
Life Sciences (School of)
Colchester Campus
Autumn
Undergraduate: Level 5
Current
Thursday 03 October 2019
Saturday 14 December 2019
15
05 September 2019

 

Requisites for this module
(none)
(none)
(none)
(none)

 

BS228

Key module for

BSC C700 Biochemistry,
BSC C701 Biochemistry (Including Placement Year),
BSC C703 Biochemistry (Including Year Abroad),
BSC CR00 Biochemistry (Including Foundation Year)

Module description

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.

Module aims

The aim of this module is to build on the basic principles of protein structure and function obtained from BS131.

Module learning outcomes

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.

Module information

No additional information available.

Learning and teaching methods

18 x 1 hour lectures, plus 1 revision class before summer exam; 2 x 3 hour practical

Bibliography

  • 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 Description Deadline Weighting
Coursework SPF 22/11/2019 100%
Exam 120 minutes during Summer (Main Period) (Main)

Overall assessment

Coursework Exam
50% 50%

Reassessment

Coursework Exam
50% 50%
Module supervisor and teaching staff
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)

 

Availability
Yes
No
No

External examiner

Dr Clive Butler
The University of Exeter
Associate Professor of Microbial Biochemistry
Resources
Available via Moodle
Of 51 hours, 21 (41.2%) 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).

 

Further information
Life Sciences (School of)

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