BGM2060 : Proteins and Enzymes

  • Module Leader(s): Prof. Bernard Connolly
  • Owning School: Biomedical Sciences
Semesters
Semester 2 Credit Value: 20
ECTS Credits: 10.0

Aims

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.

Outline Of Syllabus

The module explains the most important properties of proteins and enzymes. In particular it will examine:

protein secondary structure;
super secondary structure;
tertiary folds;
experimental measurements of protein folding;
interactions between enzymes and substrates;
enzyme catalysis;
enzyme inhibition and allosteric regulation;
transition state theory;
the mechanism of action of several biological catalysts included protein-enzymes (RNA polymerase), catalytic RNA and
catalytic antibodies.

Teaching Methods

Teaching Activities
Category Activity Number Length Student Hours Comment
Scheduled Learning And Teaching ActivitiesLecture241:0024:00N/A
Guided Independent StudyAssessment preparation and completion11:001:00Seminar
Scheduled Learning And Teaching ActivitiesPractical26:0012:00N/A
Guided Independent StudyIndependent study1163:00163:00N/A
Total200:00
Teaching Rationale And Relationship

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.

Assessment Methods

The format of resits will be determined by the Board of Examiners

Exams
Description Length Semester When Set Percentage Comment
Written Examination902A80Two essays to be answered from a choice of 4. Each essay contributes 50% of the mark
Other Assessment
Description Semester When Set Percentage Comment
Practical/lab report2M10N/A
Practical/lab report2M10N/A
Assessment Rationale And Relationship

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.

Reading Lists

Timetable

Disclaimer: The University will use all reasonable endeavours to deliver modules in accordance with the descriptions set out in this catalogue. Every effort has been made to ensure the accuracy of the information, however, the University reserves the right to introduce changes to the information given including the addition, withdrawal or restructuring of modules if it considers such action to be necessary.