Protein Structure and Function, Biospectroscopy and Bioinformatics
| Code | School | Level | Credits | Semesters |
| CHEM3004 | Chemistry | 3 | 10 | Autumn UK |
- Code
- CHEM3004
- School
- Chemistry
- Level
- 3
- Credits
- 10
- Semesters
- Autumn UK
Summary
The course will develop an understanding of protein structure, stability, de-novo design, solid phase peptide synthesis and methods of structural analysis. The correlation between structure and function in proteins will be covered. The course will present bioinformatics tools useful for structural comparison. A range of experimental spectroscopic techniques will be introduced to probe protein structure and stability based on secondary structure and tertiary interactions and to probe the nature of the active site of metalloproteins. Case-studies encompassing relevant literature on the subject will be used to highlight key aspects of the course.
Target Students
BSc/MSci Chemistry OR Medicinal and Biological Chemistry OR Natural Sciences AND for Level 3 students.
Classes
- One 1-hour workshop each week for 2 weeks
- Two 1-hour lectures each week for 9 weeks
Assessment
- 100% Exam 1 (2-hour): Second re-assessment: If a further re-assessment is allowed by satisfying the conditions of Undergraduate Course Regulation 19, the form of the further re-assessment for this module will be 100% coursework.
Assessed by end of autumn semester
Educational Aims
Students should gain an appreciation of protein secondary and tertiary structure, energetic contribution of weak interactions to protein stability, methods in de-novo design and methods of structural analysis. They should understand the protein folding problem and appreciate the range of spectroscopic methods available to probe aspects of structure and activity. Students should develop an understanding of the bioinformatics tools available to study and compare protein structure and function.Learning Outcomes
Knowledge and Understanding:
- Have an understanding of protein structure and stability and methods of structural analysis
- Understand the protein folding problem through experimental approaches
- Understand the nature of the active sites of metallo-proteins
- Be able to design peptide sequences to produce a specific folding/assembly
- Know the principles of orthogonal protection and its application in peptide synthesis
- Understand the principles of bioinformatics
Intellectual Skills:
- Ability to apply the above knowledge in novel situations
Transferable/Key Skills:
- Problem solving
- Written communication skills