Master of Chemistry (MChem)

MChem Chemistry

Gain valuable work experience as part of your Chemistry degree.
  • Duration: 4 years
  • Year of entry: 2025
  • UCAS course code: F109 / Institution code: M20
  • Key features:
  • Scholarships available
  • Accredited course

Full entry requirementsHow to apply

Course unit details:
Biomolecular Structure and Function

Course unit fact file
Unit code CHEM20722
Credit rating 10
Unit level Level 2
Teaching period(s) Semester 2
Available as a free choice unit? No

Overview

The unit is delivered by Profs David Leys, Sam Hay and Dr Neil Dixon. Each of the three elements of the course consists of 6-7 lectures and 1 to 2 workshops, and is assessed by exam + course work element.

Pre/co-requisites

Unit title Unit code Requirement type Description
Biological Chemistry CHEM10712 Pre-Requisite Compulsory

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

An understanding of the general properties of the 4 main classes of biomolecules, their general 3D structural features and how this relates to their biochemical function. A clear appreciation of the complexity of biomolecules and the emergent properties that arise from the modular design that underpins them. An ability to visualise protein:ligand complexes and correlate structure features with solution properties. This will provide you with a foundation for the further study of complex biochemical processes, biotechnological application/green chemistry and synthetic biology.

Syllabus

Prof David Leys (8 lectures + 4 workshops on macromolecular 3D visualisation)

2 lectures as Recap on Aqueous chemistry and non-covalent bonding in biology: Hydrogen bonding; Van der Waals; Ionic bonding; Hydrophobic effect; pH/pKa. Protein structure and function: amino acids; primary/secondary/tertiary/quaternary structure, folds and folding, denaturation and stability, dynamic behaviour; advanced concepts in ligand binding

6 lectures on advanced concepts in protein structure determination/modelling / protein ligand binding + workshop

Dr Neil Dixon (6 lectures)

Advanced molecular biology, Nucleotides, inherent properties and reactivity. DNA and RNA covalent and 3D structure. DNA structure – double helices, Hoogsteen base pairing. Triple helices. Base stacking. RNA structure.

Dr Sam Hay (6 lectures + workshop on mechanism/kinetic models) Advanced Biological catalysis: Enzymes introduction: Active sites,

Transferable skills and personal qualities

Problem solving skills, data mining. modelling and visualisation of complex molecular structures; communication skills.

Assessment methods

Method Weight
Written exam 80%
Written assignment (inc essay) 20%

Feedback methods

Feedback mechanisms will include direct interactions with students in the lectures as well as in the workshops. Lecturers will make themselves available via office hours or via email.

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.

 

Study hours

Scheduled activity hours
Assessment written exam 2
Lectures 23
Independent study hours
Independent study 75

Teaching staff

Staff member Role
David Leys Unit coordinator

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