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MSci Microbiology / Course details
Year of entry: 2023
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Course unit details:
|Unit level||Level 2|
|Teaching period(s)||Semester 1|
|Available as a free choice unit?||No|
Proteins are involved in virtually all biological processes and their structure is key to their function. You will learn how proteins are produced, how they fold into their secondary and tertiary structures and how they interact with each other. You will find out about the experimental techniques, such as X-ray crystallography, nuclear magnetic resonance and electron microscopy, which are used to determine the 3D structure of proteins.
|Unit title||Unit code||Requirement type||Description|
|Chemistry for Bioscientists 1||CHEM10021||Pre-Requisite||Recommended|
|Chemistry for Bioscientists 2||CHEM10022||Pre-Requisite||Recommended|
- BIOL10111 Introductory Chemistry (Recommended )
- CHEM10021/2 Chemistry for Bioscientists 1/2 (Recommended )
To provide core knowledge of the form, function and role of protein molecules in biological processes and further enable an understanding of biological phenomena at the molecular level.
Students will be able to
- Describe the features of proteins which lead to successful folding, post-translational modification and degradation.
- Describe protein folds in terms of secondary structural elements and the restrictions on peptide structure imposed by the planarity of the peptide bond.
- Select appropriate experimental techniques for protein purification and characterization (conformation and stability), and describe the relative precision of various approaches and the assumptions implied by each method.
- Outline methods for 3D structure determination by X-ray crystallography, NMR and electron microscopy.
- Analyze and manipulate structural data (including the use of the Protein Data Bank in Europe).
- Analyze data relating to protein function and demonstrate an understanding of associated variables (resolution, Kd, Km & Vmax).
- Distinguish between various modes of protein-protein interaction and catalysis.
Course material can be divided into three broad themes and will comprise lectures on (1) Protein folding and modification, protein isolation, identification and characterization; (2) Methods for protein structure determination and rational modelling (including an interactive computer workshop); (3) Protein interactions and enzyme characterization.
Each of the themes outlined above will be supported by Blackboard eLearning modules each including an online quiz and discussion board. The interactive computer workshops associated with theme (2) will be complemented by a formative Blackboard modules.
- Analytical skills
- There is considerable use of graphs and underlying theory in the description of properties of proteins and how these are studied.
- Group/team working
- Group discussions on the aforementioned boards may be used to supplement private study in groups. A number of in-class exercises are undertaken and additional exercises are provided on the Blackboard site - these can be attempted as group exercises.
- Project management
- There are regular on line assessments, students must keep pace with the course in order to achieve a good outcome here.
- Oral communication
- Students ask questions in lectures; interact with teaching staff in 2 microlab workshops and participate in a wrap up Q&A lecture at the end of the course.
- Problem solving
- Problem solving is developed quite extensively, supported by the on-line exercises; problem driven computer workshops and examples.
- There are case study type examples in the course which are directly relevant to research, databases are explored in computer classes which are invaluable in support of research. The emphasis of the course is on practical applications, for example selecting the best technique to address a particular question on protein structure and function.
- Written communication
- There are discussion boards on Blackboard on specific themes and students are encouraged to use these in support of their studies.
- Many of the skills first encountered in the Proteins unit are reinforced in the Biochemistry/Medical Biochemistry semester 4 tutorial program. A large subset of the students therefore extend their skills in smaller teams in tutorials, where they are required to relate and apply the material from Proteins in a problem-solving environment. These thematic tutorials are assessed by the submission of short reports.
BIOL21111.1 Online ePBL - Protein folding - 5% Week 3
BIOL21111.2 Online ePBL - Protein Characterization - 5% - Week 5
BIOL21111.3 Online ePBL - Ligand Binding - 5% - Week 7
BIOL21111.4 Online ePBL - Catalysis - 5% - Week 9
BIOL21111.5 Online ePBL - Structure Determination - 5% - Week 12
BIOL21111.6 Final Unit exam - 2 hour written examination (30 minutes assigned for question reading and choice of question). 1 essay type answer from a total of 2 integrative questions. Remote exam. 75%.
Feedback will be provided directly via online discussion boards and through comments in response to practise questions associated with the Blackboard e-learning modules, the mark for assessed Blackboard components is also given as soon as the assignment is completed. Interactive feedback is also provided during the computer workshops at the end of the course. A drop-in session for reviewing marked exam scripts will also be arranged.
All lecturers provide supporting handouts, the following textbooks may give additional perspectives. Links to Library entries for these are provided within the course Blackboard site.
Exploring proteins: a student's guide to experimental skills and methods - Price, Nicholas C., Nairn, Jacqueline 2009
Proteins: structure and function - Whitford, David 2003
|Scheduled activity hours|
|Assessment written exam||2|
|Independent study hours|
|Stephen Prince||Unit coordinator|
students need only take one of recommended pre-requisite CHEM10021 OR CHEM10022