- UCAS course code
- F109
- UCAS institution code
- M20
Master of Chemistry (MChem)
MChem Chemistry
Duration: 4 years
Year of entry: 2025
UCAS course code: F109 / Institution code: M20
- Key features:
Scholarships available
Accredited course
- Typical A-level offer: A*AA including specific subjects
- Typical contextual A-level offer: AAA including specific subjects
- Refugee/care-experienced offer: AAB including specific subjects
- Typical International Baccalaureate offer: 37 points overall with 7,6,6 at HL, including specific requirements
Course unit details:
Biomolecular Structure and Function 2
| Unit code | CHEM30722 |
|---|---|
| Credit rating | 10 |
| Unit level | Level 3 |
| Teaching period(s) | Semester 2 |
| Available as a free choice unit? | No |
Overview
This course unit detail provides the framework for delivery in 22/23 and may be subject to change due to any additional Covid-19 impact.
The unit is delivered by Profs David Leys and Jon Waltho (X-ray and NMR), Dr. Jim Warwicker (modelling) and Dr. Anthony Green (protein:ligand interactions). Each of the three elements of the course consists of 6-7 lectures and 1 to 2 workshops, and is assessed by exam and a small element of coursework.
Pre/co-requisites
| Unit title | Unit code | Requirement type | Description |
|---|---|---|---|
| Biomolecular Structure and Function | CHEM20722 | Pre-Requisite | Recommended |
Aims
The unit aims to look at protein structure and function relationship in detail, with a focus on looking at proteins relevant to the chemistry (ie mainly enzymes) and consisting of three elements: protein 3D structure determination, protein modelling studies and protein:ligand interactions. The latter aims to look at the importance of non-covalent interactions in chemical and biological systems, and describe some applications in modern chemical research.
Learning outcomes
On successful completion of the course students should be able to:
(i) understand the main methodology underpinning X-ray/NMR structure determination and the implications this has for the relevance/accuracy and information content of the corresponding protein structure models
(ii) understand the scope and limitations of protein structure and protein driven process energetics modelling
(iii) Understand non-covalent interactions and their importance in chemical and biological systems
Transferable skills and personal qualities
Problem solving skills, data mining. modelling and visualisation of complex molecular structures; communication skills (through submission of written course work)
Assessment methods
| Method | Weight |
|---|---|
| Written exam | 85% |
| Written assignment (inc essay) | 15% |
Feedback methods
Feedback mechanisms will include direct interactions with students in the lectures as well as in the workshops. A small element of marked coursework for each of the three sections will provide detailed feedback on the students progress and understanding of the topic matter.
Recommended reading
The recommended text for this course is Voet & Voet Biochemistry, 4th Edition, Wiley. Earlier editions of this text also contain the relevant content. Other review articles relevant to material will be provided.
Study hours
| Scheduled activity hours | |
|---|---|
| Assessment written exam | 2 |
| Lectures | 20 |
| Practical classes & workshops | 2 |
| Independent study hours | |
|---|---|
| Independent study | 76 |
Teaching staff
| Staff member | Role |
|---|---|
| David Leys | Unit coordinator |