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DRPS : Course Catalogue : School of Biological Sciences : Postgraduate

Postgraduate Course: Protein Production for Therapeutic Discovery (PGBI11132)

Course Outline
SchoolSchool of Biological Sciences CollegeCollege of Science and Engineering
Credit level (Normal year taken)SCQF Level 11 (Postgraduate) AvailabilityNot available to visiting students
SCQF Credits20 ECTS Credits10
SummaryThe core methods and technologies being implemented for modern production and purification will be discussed and illustrated. The type and configuration of the instrumentation used in modern protein production labs will be discussed as well as the practical considerations for development of effective methods on such equipment. Real world examples will be used as exemplars for best practice in strategy development.

In the practical element of the course, students will get a thorough hand-on instruction/training in the chromatographic and processing methods involved in purifying a recombinantly expressed therapeutically valuable/relevant protein to homogeneity. Using LDH-A as the model system, the course will apply a range of techniques to extract and then purify the material to homogeneity. Students will be exposed to several methods of extraction and chromatographic methodologies: IMAC and GF. They will utilise modern LC equipment (AKTA Start system) to perform the purification.
Course description In the development of new therapeutics, structure determination is vital part of the pipeline of discovery. This relies heavily on the supply of suitable high quality protein material. The automation and technological developments in the platforms utilised for structural determination (X-ray diffraction, NMR or Cyro-EM) has miniaturised the process and increased the throughout, with less material. However, this has increased the need for the development of rapid, effective, and reproducible processes for the expression, purification of proteins and protein therapeutics.

The core methods and technologies being implemented for modern production and purification will be discussed and illustrated. The type and configuration of the instrumentation used in modern protein production labs will be discussed as well as the practical considerations for development of effective methods on such equipment. Real world examples will be used as exemplars for best practice in strategy development, with a focus on newer biologic molecule entities.

In the practical elements of the course, students will get a hands-on instruction in the chromatographic and processing methods involved in purifying a recombinantly expressed therapeutically valuable protein to homogeneity. Students will be exposed to several methods of extraction different types of chromatographic methodologies. A major aspect of the course is teaching the students how to adapt applicable methods for assessing activity and purify and biophysical coherency of their sample throughout the purification process, based on the behaviour of real-world sample and available resources. This is important for both traditional drug discovery programs where the protein may be the target, as well the modern trend where the target is the therapeutic itself.
Entry Requirements (not applicable to Visiting Students)
Pre-requisites Co-requisites
Prohibited Combinations Students MUST NOT also be taking Practical Skills in Biochemistry B (PGBI11099) OR Protein Production for Therapeutic Discovery (Biochemistry) (BICH11010)
Other requirements None
Course Delivery Information
Academic year 2024/25, Not available to visiting students (SS1) Quota:  24
Course Start Full Year
Timetable Timetable
Learning and Teaching activities (Further Info) Total Hours: 200 ( Lecture Hours 6, Seminar/Tutorial Hours 6, Supervised Practical/Workshop/Studio Hours 24, Feedback/Feedforward Hours 2, Formative Assessment Hours 2, Programme Level Learning and Teaching Hours 4, Directed Learning and Independent Learning Hours 156 )
Assessment (Further Info) Written Exam 0 %, Coursework 100 %, Practical Exam 0 %
Additional Information (Assessment) ICA:
Semester 1:
Presentation on a methods paper (30%)
Report following ProteinLab practical (30%)

Semester 2:
Report in the form of a research paper (40%)
Feedback In tutorials and formative assessments there will be small scale assignments to be completed for the tutorial, and these would feedback how the student was doing. Feedback from ICA 1 & 2 and formative sessions will be useful in informing student of how their descriptive abilities could be improved for ICA 3.
No Exam Information
Learning Outcomes
On completion of this course, the student will be able to:
  1. Be familiar with all common methods or production, primary processing, and purification.
  2. Apply a range of chromatographic and extraction techniques to purify and process proteins.
  3. Demonstrate ability to design and implement a multi-step purification protocol and suggest applicable biophysical methods for assessment of sample purity and activity.
  4. Demonstrate the ability to operate modern LC instrumentation and apply dynamic strategies for alteration/adaptation of standard methods based on the behaviour of real samples.
  5. Demonstrate good working practice in a modern wet lab and keeping appropriate documentation/lab books.
Reading List
None
Additional Information
Graduate Attributes and Skills Knowledge and understanding: Key aspects of protein purifications techniques.
Technical and Practical Skills: implementation of the skills given in theoretical section.
Personal and Intellectual Autonomy: course requires extensive external reading and ability to integrate this material with taught material, and present it effectively.
Communication: Students learn to communicate details of an experimental protocol through presentation.
KeywordsNot entered
Contacts
Course organiserDr Martin Wear
Tel: (0131 6)50 7054
Email: Martin.Wear@ed.ac.uk
Course secretaryMiss Fionnuala Nidhonnabhain
Tel:
Email: fnidhonn@ed.ac.uk
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