BGM2060 : Proteins and Enzymes
BGM2060 : Proteins and Enzymes
- Offered for Year: 2024/25
- Module Leader(s): Dr David Bolam
- Lecturer: Professor Jane Endicott, Professor Wyatt Yue, Dr Jon Marles-Wright, Professor David Elliott, Dr Elizabeth Veal
- Owning School: Biomedical, Nutritional and Sports Scien
- Teaching Location: Newcastle City Campus
Semesters
Your programme is made up of credits, the total differs on programme to programme.
Semester 2 Credit Value: | 20 |
ECTS Credits: | 10.0 |
European Credit Transfer System | |
Pre-requisite
Modules you must have done previously to study this module
Pre Requisite Comment
BMS Phase 1 Core Modules.
Co-Requisite
Modules you need to take at the same time
Co Requisite Comment
None
Aims
The aim of the module is to provide students with a detailed understanding of protein structure, function and application, with particular focus on enzymes.
Outline Of Syllabus
•Properties of proteins and enzymes, macromolecules essential to all life.
•Protein secondary structure, super secondary structure and tertiary folds and introduce key concepts in protein folding, including intrinsically unfolded proteins.
•Specific interactions between enzymes and substrates are determined by protein structure and how preferential binding of the transition state by enzymes leads to catalysis
•Kinetic parameters that describe enzyme catalysis, inhibition and allosteric regulation
•Mechanisms of action of several major enzyme classes to illustrate key catalytic strategies.
•The concept that a protein can carry out more than one function ('moonlighting' proteins)
•Catalysis by RNA and comparison to protein enzymes.
Learning Outcomes
Intended Knowledge Outcomes
On completion of the module students will be able to:
1. Discuss advanced aspects of protein biochemistry such as protein structure and folding.
2. Explain the quantitative determination and significance of enzyme steady-state kinetic parameters.
3. Discuss the structural basis of enzyme catalysis and substrate specificity, and the contribution of kinetic and physical experiments to an understanding of these properties.
4. Describe the different mechanisms by which enzymes can be inhibited by small molecules and the importance of enzyme inhibitors as drugs and toxins.
5. Describe how allosteric properties are related to protein structure.
6. Understand that a single protein can carry out multiple functions.
7. Illustrate and compare the enzymology of selected biological catalysts, including RNA.
8. Solve quantitative and conceptual problems in each of these topics.
Intended Skill Outcomes
On completion of the module students will be able to:
1. Generate, analyse and interpret experimental data.
2. Solve quantitative and conceptual problems in enzymology.
3. Generate reports.
Teaching Methods
Teaching Activities
Category | Activity | Number | Length | Student Hours | Comment |
---|---|---|---|---|---|
Scheduled Learning And Teaching Activities | Lecture | 20 | 1:00 | 20:00 | In person on campus |
Guided Independent Study | Assessment preparation and completion | 1 | 80:00 | 80:00 | Preparation and completion of lab reports and exam revision |
Scheduled Learning And Teaching Activities | Practical | 1 | 7:00 | 7:00 | In person on campus |
Scheduled Learning And Teaching Activities | Practical | 1 | 6:00 | 6:00 | In person on campus |
Scheduled Learning And Teaching Activities | Small group teaching | 1 | 2:00 | 2:00 | In peron on campus. Revision seminar to provide opportunities for discussion and clarification of module |
Scheduled Learning And Teaching Activities | Small group teaching | 3 | 1:00 | 3:00 | In person seminars - Practical write up guidance and feedback sessions |
Guided Independent Study | Independent study | 1 | 82:00 | 82:00 | Writing up lecture notes, revision and general reading |
Total | 200:00 |
Teaching Rationale And Relationship
The lectures will cover the key points of the module and will be reinforced by the practicals. Seminars offer students an opportunity to discuss their understanding and check their learning against the module outcomes.
The practicals form the core of this module as they will give the students ‘hands-on’ experience of key methods in protein biochemistry, and provide training in data acquisition, interpretation and critical analysis.
Reading Lists
Assessment Methods
The format of resits will be determined by the Board of Examiners
Exams
Description | Length | Semester | When Set | Percentage | Comment |
---|---|---|---|---|---|
Written Examination | 90 | 2 | A | 70 | In person invigilated Exam. 4 short answer questions. All questions to be answered |
Other Assessment
Description | Semester | When Set | Percentage | Comment |
---|---|---|---|---|
Practical/lab report | 2 | M | 15 | 1,600 words |
Practical/lab report | 2 | M | 15 | 1,200 words |
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 teamwork skills (students will work in groups of 2) and general laboratory skills.
The practical write up tests data analysis, critical thinking and report-writing skills.
Timetable
- Timetable Website: www.ncl.ac.uk/timetable/
- BGM2060's Timetable
Past Exam Papers
- Exam Papers Online : www.ncl.ac.uk/exam.papers/
- BGM2060's past Exam Papers
General Notes
Original Handbook text:
Welcome to Newcastle University Module Catalogue
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Disclaimer
The information contained within the Module Catalogue relates to the 2024 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 2025/26 entry will be published here in early-April 2025. Queries about information in the Module Catalogue should in the first instance be addressed to your School Office.