|Semester 2 Credit Value:||20|
Stage 1, Stage 2 semester 2. That is, BGM1001, CMB1000, CMB1001, PSC1001, BGM1003,
PED1002, CMB2002, CMB2003, CMB2004, CMB2005.
1. To explore the dynamic and varied world of proteins from a structural point of view.
2. To explain protein folding and how the correctly folded state is achieved.
3. To illustrate the methods used to study protein folding and characterisation of correct folding.
4. To show how enzymes recognise substrates and other molecules, leading to catalysis, inhibition and allosteric regulatory properties.
5. To explain steady state enzyme kinetics in quantitative terms.
6. To emphasise the importance of transition state stabilisation by enzymes.
7. To discuss the mechanism of action of selected enzymes in detail.
8. To introduce the concepts of catalytic RNA and catalytic antibodies.
9. To illustrate that enzymes have important industrial and medical application.
10. To provide an opportunity to interpret and discuss original research publications.
The module explains the most important properties of proteins and enzymes, macromolecules of critical importance and significance to all cell-based life. The module will examine protein secondary structure, super secondary structure and tertiary folds and introduce protein folding, discussing why proteins are the shape they are. The module will also explain how specific interactions between enzymes and substrates are determined by protein structure and how substrate binding leads to enzyme catalysis. The module will develop students' understanding of the kinetic parameters that describe enzyme catalysis, inhibition and allosteric regulation. Students are introduced to transition state theory and it is explained how specific binding of the transition state by enzymes leads to catalysis. The module concludes with an in depth examination of the mechanism of action of several biological catalysts included protein-enzymes (enzymes useful in bioenergy production and enzymes that are targets for influenza anti-virals), catalytic RNA and catalytic antibodies.
The module explains the most important properties of proteins and enzymes. In particular it will examine:
protein secondary structure;
super secondary structure;
experimental measurements of protein folding;
interactions between enzymes and substrates;
enzyme inhibition and allosteric regulation;
transition state theory;
the mechanism of action of several biological catalysts included protein-enzymes (RNA polymerase), catalytic RNA and
1. Show understanding of advanced aspects of protein biochemistry such as protein structure and folding.
2. Show skills needed to understand biological macromolecules, especially proteins.
3. Explain the quantitative determination and significance of enzyme steady-state kinetic parameters and to describe how allosteric properties are related to protein structure.
4. Discuss the structural basis of enzyme catalysis and substrate specificity, and the contribution of kinetic and physical experiments to an understanding of these properties.
5. Understand transition state theory and its importance in enzyme catalysis.
6. Have a detailed understanding of the enzymology of selected proteins.
7. Appreciate how transition state theory has lead to catalytic antibodies.
8. Show an understanding of the distinctive characteristics of RNA catalysis.
9. Solve quantitative and conceptual problems in each of these topics.
Skills for solving quantitative and conceptual problems in each of these topics
General laboratory skills
General laboratory skills
|Graduate Skills Framework Applicable:||Yes|
|Guided Independent Study||Assessment preparation and completion||1||1:00||1:00||Seminar|
|Scheduled Learning And Teaching Activities||Lecture||24||1:00||24:00||N/A|
|Scheduled Learning And Teaching Activities||Practical||2||6:00||12:00||N/A|
|Guided Independent Study||Independent study||1||163:00||163:00||N/A|
The lectures will cover the key points of the module and will be reinforced by the seminar session and the practicals. The practicals form the core of this module as they will give the students ‘hands-on’ experience of the key methods discussed in the lectures, and also bring together other learning outcomes.
The format of resits will be determined by the Board of Examiners
|Written Examination||90||2||A||80||Two essays to be answered from a choice of 4. Each essay contributes 50% of the mark|
Exams test all knowledge across the module.
Practicals assess students understanding of key points in the lectures, ability to report and analyse results, and tests their team work (students will work in groups of 2 or more) skills and general laboratory skills.
The two practical sessions:
RL: Purification, crystallisation and structural analysis of egg-white lysozyme (6 hours)
CD: Determination of the type of inhibition of fumarase by succinate (6 hours)
The RL sessions will give the students practical experience of the modern protein purification techniques introduced in
the lectures. The practical run by CD will give the students the opportunity to generate their own enzymatic data for
analysis, and reinforce their laboratory skills, along with introducing modern enzymatic techniques.
Original Handbook text:
Disclaimer: The information contained within the Module Catalogue relates to the 2016/17 academic year. In accordance with University Terms and Conditions, the University makes all reasonable efforts to deliver the modules as described. Modules may be amended on an annual basis to take account of changing staff expertise, developments in the discipline, the requirements of external bodies and partners, and student feedback. Module information for the 2017/18 entry will be published here in early-April 2017. Queries about information in the Module Catalogue should in the first instance be addressed to your School Office.