Module Information

Module Identifier
Module Title
Academic Year
Semester 1
Other Staff

Course Delivery

Delivery Type Delivery length / details
Lecture 3 x 1 hour lectures per week
Practical 2 x 3 hour practicals per semester


Assessment Type Assessment length / details Proportion
Semester Assessment Assignment  Essay  20%
Semester Assessment Practical report  20%
Semester Exam 2 Hours   Written examination  60%
Supplementary Assessment Supplementary assignment  20%
Supplementary Assessment Practical report  20%
Supplementary Exam 2 Hours   Supplementary examination  60%

Learning Outcomes

On successful completion of this module students should be able to:

Recognize the formulae of the amino acids found in proteins and to describe the importance of the type of side-chain to protein structure and function.

Define how the amino acid sequence contributes to other levels of protein structure and of the mechanism of protein folding.

Recount a variety of post-translational modifications of proteins and describe the processes which govern the targeting of proteins to specific organelles within the cell.

Explain what enzymes do, how they are assayed and how they can be isolated. Students should also be able to manipulate kinetic data to infer relevant parameters of enzymatic reactions.

Perform experimental protocols for the manipulation and characterisation of proteins, and to report hte results of such experimental investigations clearly and concisely.


The course is designed to extend and reinforce those aspects of protein structure dealt with in the first year with current ideas on the folding of nascent proteins and the post-translational modifications, to give the students a firm understanding of the relationship between structure and function.


The module begins with a survey of the wide range of protein function with examples given for each. The next section deals with protein structure starting with the amino acid building blocks with a reminder of the importance of pH in the role of charged groups in protein structure and function.

The structure of some biologically active small peptides are described before the course moves on to deal with the polypeptides as found in proteins and considers their primary structure and its elucidation. The students will be reminded of the special features of the peptide bond that lead to secondary structure and of the main types of secondary structure, a-helix, b-pleated sheet and the collagen triple helix. This leads on to a consideration of tertiary and quaternary structures, their stabilisation and importance to function, with haemoglobin used as the main example. The process of protein folding to give a functional structure and the way in which proteins are targeted to cell compartments will be described. Aspects of post-translational modification of proteins will also be dealt with.

Several lectures will cover basic aspects of catalysis, enzyme nomenclature, enzyme assay, simple enzyme kinetics, inhibition of enzymes and some aspects of control. The ways in which enzymes might bring about catalysis are examined with a more detailed look at chymotrypsin to illustrate these points.

The final section deals with aspects of protein purification. Procedures for estimation of protein purity and the protocol for documentation of a purification are described.

As part of their individual studies the students are expected to work through the chapters on pH in the appropriate textbooks and to become familiar with calculations in this topic by attempting the numerical problems at the end of these chapters. Further individual study may be supplemented by on-line tutorials and testing provided by the text associated with Stryer, see below. Students are also expected to familiarise themselves in this way with quantitative aspects of enzyme assays, particularly by use of spectrophotometry, and enzyme kinetics.

Module Skills

Skills Type Skills details
Application of Number Interpretation of kinetic data and numerical analysis of protein purification requires development of numeric skills.
Communication Listening skills for the lectures. Students will develop effective written communiction skills in examinations and in coursework preparation.
Improving own Learning and Performance Outside the formal contact hours, students will be expected to research materials, manage time and meet deadlines. The directed study elements will provide opportunity for students to explore their own learning styles and preferences and indentify their needs and barriers to learning. Students will be able to review and monitor their progress and plan for improvement of personal performance.
Information Technology Accessing the web for information sources and using databases to find primary literature.
Personal Development and Career planning Students will gain confidence in their ability to evaluate biological problems and objectively assess the quality of proposed solutions.
Problem solving Through the lectures students will become aware of the structure and function of proteins and enzymes. Lectures will explain designing and executing experiments with protein and guidance on interpreting kinetic data in enzymology
Research skills Students will research topics beyond the depth and scope of the lecture material, using both directed and independent study. Information from a variety of sources will be the object of scrutiny and comment.
Subject Specific Skills Subject specific concepts relating to protein biochemistry and enzymology will be developed. Students will be able to demonstrate an understanding of integrated structure and function of proteins and evaluate pertinent protein properties.
Team work Students will work in pairs/small groups during practical sessions. They will need to discuss their experimental design and work effectively as a small team in practical classes

Reading List

Recommended Text
Berg, J.M., Tymoczko, J.L., & Stryer, L. (2002) Biochemistry 5th Freeman Primo search


This module is at CQFW Level 5