|Delivery length / details
|22 x 1 Hour Lectures
|1 x 4 Hour Practical
|Assessment length / details
|Students must take elements of assessment equivalent to those that led to failure of the module.
|2 Hours Students must take elements of assessment equivalent to those that led to failure of the module.
On successful completion of this module students should be able to:
1. Define how the amino acid sequence contributes to other levels of protein structure and of the mechanism of protein folding.
2. 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.
3. Explain how enzymes are assayed and how they can be isolated. Student should also be able to manipulate kinetic data to infer relevant parameters of enzymatic reactions.
4. Perform experimental protocols for the manipulation and characterisation of proteins, and to report the 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 post-translational modifications, to give the students a firm understanding of the relationship between structure and function.
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. 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 specific examples to illustrate these points.
A final section deals with aspects of protein purification and methods for studying proteins. Procedures for estimation of protein purity and the protocol for documentation of a purification are described.
Practical experience of working with and characterising proteins and enzymes will also be provided, through laboratory practical sessions.
|Application of Number
|Interpretation of kinetic data, and numerical analysis of protein purification requires development of numeric skills
|Listening skills for the lectures. Students will develop effective written communication 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 identify their needs and barriers to learning. Students will be able to review and monitor their progress and plan for improvement of personal performance.
|Accessing the web for information sources and using databases to find primary literature, preparation of coursework.
|Personal Development and Career planning
|Practical classes will allow students to gain experience in designing and executing experiments, and in interpreting data in biochemistry.
|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.
This module is at CQFW Level 5