Postgraduate Course: Preparative Methods for Structural Biology (PGBI11026)
Course Outline
| School | School of Biological Sciences |
College | College of Science and Engineering |
| Credit level (Normal year taken) | SCQF Level 11 (Postgraduate) |
Availability | Available to all students |
| SCQF Credits | 10 |
ECTS Credits | 5 |
| Summary | As structure determination of proteins relies heavily on the supply of suitable protein material, the preparative and analytical methods leading up to X-ray diffraction, NMR or Cyro-EM experiments, for example, are of eminent importance. Commonly utilised methods of, expression, purification of proteins will be discussed. The type and configuration of the instrumentation used in modern protein production labs will be discussed as well as the practical considerations for writing methods on such equipment. As a course outcome, the students should be familiar with all common methods and be able to start practical work with recombinant proteins. |
| Course description |
Lecture Outlines
Week 1 Course requirements / assessment / introduction to protein production and purification theory.
Week 2 Production / Purification theory.
Week 3 Applications; Purification Strategies and Examples-1.
Week 4 Applications; Purification Strategies and Examples-2.
Week 5 Solubilisation / Re-folding Strategies for Insoluble Recombinant Proteins.
Week 6 Design a purification Protocol.
Week 7 ProteinLab Computer Practical pt1.
Week 8 ProteinLab Computer Practical pt2.
Week 9 Round off session 1 / assessment slot 1
Week 10 Round off session 2 / assessment slot 2
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Entry Requirements (not applicable to Visiting Students)
| Pre-requisites |
|
Co-requisites | |
| Prohibited Combinations | |
Other requirements | Entry to the course will be for students already holding (or expecting to hold) an Honours degree or equivalent in a biological subject such as biochemistry, molecular biology, biophysics, pharmacology. Students with a background in chemistry, physics, computer science or informatics will also be considered and those with other scientific or medical backgrounds should contact the Course Organiser. |
| Additional Costs | None |
Information for Visiting Students
| Pre-requisites | None |
| High Demand Course? |
Yes |
Course Delivery Information
|
| Academic year 2017/18, Available to all students (SV1)
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Quota: None |
| Course Start |
Semester 1 |
Timetable |
Timetable |
| Learning and Teaching activities (Further Info) |
Total Hours:
100
(
Lecture Hours 30,
Programme Level Learning and Teaching Hours 2,
Directed Learning and Independent Learning Hours
68 )
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| Assessment (Further Info) |
Written Exam
0 %,
Coursework
100 %,
Practical Exam
0 %
|
| Feedback |
Not entered |
| No Exam Information |
Learning Outcomes
On completion of this course, the student will be able to:
- know of and appreciate commonly used strategies for protein production for structural biology and analytical biochemical assays.
- understand and assimilate data relating to protein production and purification methodology design and execution.
- understand and extract context specific information about the method used and the post-run processing options from a protein purification LC chromatogram.
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Reading List
Recommended Reading
- Protein Purification Techniques: A Practical Approach (Practical Approach Series). 2nd Edition. Simon Roe, Ed.
- Protein Purification Applications: A Practical Approach. 2nd Edition. Simon Roe, Ed.
- Protein purification: principles, high-resolution methods, and applications. 2nd Edition. Jan-Christer Janson, Lars Rydén.
Advised Preparatory Work
All students should endeavour to learn the structures and basic biophysical properties of all the amino acids and nucleotide bases before the course starts. |
Additional Information
| Graduate Attributes and Skills |
Not entered |
| Keywords | PrepMethodSB |
Contacts
| Course organiser | Dr Martin Wear
Tel: (0131 6)50 7054
Email: |
Course secretary | Miss Sarah Harvey
Tel: (0131 6)51 7052
Email: |
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