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Proteins Architecture & Action - CHE00022I

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  • Department: Chemistry
  • Module co-ordinator: Prof. Tony Wilkinson
  • Credit value: 10 credits
  • Credit level: I
  • Academic year of delivery: 2018-19

Module summary

This module concerns the most versatile class of biological molecules - proteins. The first parts of the module cover protein structure, stability and folding including consideration of techniques used to study proteins. The second half of the module concerns the diverse activities of proteins and how structure gives rise to function including detailed case studies.


Module will run

Occurrence Teaching cycle
A Spring Term 2018-19 to Summer Term 2018-19

Module aims

This module explores advanced aspects of protein science – including protein structure and function, determination of structure and protein engineering. Our appreciation of almost all aspects of biochemistry and molecular biology has been enhanced by the elucidation of atomic resolution structures that reveal the underlying chemical mechanisms responsible for biological function. In addition, our ability to exploit this understanding through the use of genetic approaches to engineer proteins, is leading to the generation of improved proteins for therapeutic and biotechnology applications. Students studying this module will be equipped to go on to further studies in biochemistry/molecular biology related fields of study, as well as having valuable insight into the growing biotechnology sector of industry.

Module learning outcomes

Students will:

  • understand the basic principles of how protein structures are determined using the methods of X-ray crystallography, NMR spectroscopy and cryo-electron microscopy
  • appreciate how protein structure relates to protein mechanism and thus to biological function.
  • understand how the relationship between sequence, structure and function can be exploited to model the structure of homologous proteins
  • learn about the wide range of functions which can be performed by proteins – such as enzymes, signalling proteins, membrane bound transport proteins and structural proteins. Students will be expected to rationalise and understand the behaviour of different proteins based on their structural features.
  • engage with case studies to cement their understanding of the key topics.

Module content

The module is focussed on proteins, the most versatile of all molecules. After a discussion of the main features of protein structure, the course will cover the determination of 3D structure through X-ray diffraction, electron microscopy and NMR spectroscopy. After a brief discussion of the patterns that are emerging in protein structure (and how this can be exploited to predict protein structure), the course concludes with some examples of proteins in action.

Introduction:  1 lecture AJW (1)

Determining Protein Structure and Stability: 9 lectures  KSW (4),  MJP (3)  AAA (2) 

Techniques of Structure Determination

  • Protein Crystallography
  • NMR Spectroscopy
  • Cryo-Electron Microscopy
  • Circular Dichroism Spectroscopy and Protein Folding

Protein Structure and Diversity:  3 lectures.  (REH 3)

  • Essential features of protein structure and the forces involved in protein folding and assembly.
  • Relationship between sequence, structure and function - generating models of homologous proteins.

The function of proteins in biological systems.  5 lectures :  REH (2) AAA (3)

  • Proteins as Enzymes - Protein Kinases and Proteins as Switches,
  • DNA translocating motors and viruses.

The course contains 2 Workshops in which Molecular Graphics will be used. The first will feature Electron Density Map Fitting and the second will explore the Structural Basis of Enzyme Action

Assessment: Workshop assessment: 1 x 3.5 hour Assessed Computational Workshop on Structural Basis of Enzyme Action. Closed examination: students answer one compulsory question.


Task Length % of module mark
Assessed Workshop: Structural Basis of Enzyme Action
3.5 hours 20
University - closed examination
Proteins Architecture & Action Exam
1 hours 80

Special assessment rules



Task Length % of module mark
Assessed Workshop: Structural Basis of Enzyme Action
3.5 hours 20
University - closed examination
Proteins Architecture & Action Exam
1 hours 80

Module feedback

Students will receive feedback on their performance in the workshop assessments. They will receive verbal feedback on their progress in the formative workshops, which support lectures.

The closed examinations held in the Summer term are marked typically within 4 weeks with mark slips (with per-question break-down) being returned to students via supervisors in week 10 of the Summer Term. Outline answers are made available via the Chemistry web pages when the students receive their marks, so that they can assess their own detailed progress/achievement. The examiners reports for each question are made available to the students via the Chemistry web pages.

Indicative reading

To be provided by individual tutors

The information on this page is indicative of the module that is currently on offer. The University is constantly exploring ways to enhance and improve its degree programmes and therefore reserves the right to make variations to the content and method of delivery of modules, and to discontinue modules, if such action is reasonably considered to be necessary by the University. Where appropriate, the University will notify and consult with affected students in advance about any changes that are required in line with the University's policy on the Approval of Modifications to Existing Taught Programmes of Study.