Syllabus for Protein Engineering
A revised version of the syllabus is available.
- 15 credits
- Course code: 1BG301
- Education cycle: Second cycle
Main field(s) of study and in-depth level:
Applied Biotechnology A1F,
Explanation of codes
The code indicates the education cycle and in-depth level of the course in relation to other courses within the same main field of study according to the requirements for general degrees:
- G1N: has only upper-secondary level entry requirements
- G1F: has less than 60 credits in first-cycle course/s as entry requirements
- G1E: contains specially designed degree project for Higher Education Diploma
- G2F: has at least 60 credits in first-cycle course/s as entry requirements
- G2E: has at least 60 credits in first-cycle course/s as entry requirements, contains degree project for Bachelor of Arts/Bachelor of Science
- GXX: in-depth level of the course cannot be classified
- A1N: has only first-cycle course/s as entry requirements
- A1F: has second-cycle course/s as entry requirements
- A1E: contains degree project for Master of Arts/Master of Science (60 credits)
- A2E: contains degree project for Master of Arts/Master of Science (120 credits)
- AXX: in-depth level of the course cannot be classified
- Grading system: Fail (U), Pass (3), Pass with credit (4), Pass with distinction (5)
- Established: 2007-03-15
- Established by:
- Revised: 2019-10-25
- Revised by: The Faculty Board of Science and Technology
- Applies from: Autumn 2020
150 credits including (1) Molecular Cell Biology, or Functional Genomics, or Molecular Infection Biology, or Genome Biology, or (2) 30 credits within the Master's Programme in Applied Biotechnology, the Master's Programme in Molecular Biotechnology or Master's Programme in Chemistry with Specialisation in Biochemistry. Proficiency in English equivalent to the Swedish upper secondary course English 6.
- Responsible department: Biology Education Centre
During the course, the students work on a current molecular biological and gene technological problem. The aim is to provide advanced knowledge and skills that enable the students to find solutions on their own, and put these solutions into practice.
On completion of the course, the student should be able to:
- analyse the structure and construction of proteins by computer-based methods
- describe the structure and classification of proteins
- analyse and compare the amino acid sequence and structure of proteins, and relate this information to the function of proteins
- outline the characteristics of individual amino acids and their effect on the solubility, structure and function of proteins
- review factors significant for protein folding processes and stability
- explain how proteins can be used for different industrial and academic purposes such as structure determination, organic synthesis and drug design
- analyse the purity and stability of proteins and explain how to store them in the best way
- describe how one can use biotechnical methods to construct plasmids for the expression of natural and modified genes
- plan mutagenesis experiments to test protein stability and/or function
- design primers to introduce mutations by means of PCR
- carry out a PCR-based mutagenesis experiment
- isolate proteins by biochemical methods
- plan and carry out activity measurements of isolated proteins and characterise their purity and stability
- keep a complete and informative lab journal, with an understanding of the requirements for GLP
- design a simple research plan for a biotechnological invention
Lectures and computer-based exercises covering biotechnological methods and the structure and function of proteins. Lectures about industrial and other applications. Project-based biotechnological experiments,including production and analysis of modified proteins.
The students will document their laboratory activities, which is aimed to prepare them for the demands of future employment. The student will also propose novel solutions to a chosen biotechnical problem.
The course consists of lectures, guest lectures, seminars, group work, computer and laboratory sessions. Participation in seminars, laboratory sessions and connected lectures, group work, tests and computer exercises is compulsory.
Modules: Theory (7 credits); Practicals (8 credits)
The theory module is examined through written exams, as well as oral and written assignments (7 credits).
The practical module requires a correctly kept laboratory journal, and oral presentations of wet lab experiments (5 credits), as well asan oral presentation of an original research project (3 credits).
If there are special reasons for doing so, an examiner may make an exception from the method of assessment indicated and allow a student to be assessed by another method. An example of special reasons might be a certificate regarding special pedagogical support from the disability coordinator of the university.
- Latest syllabus (applies from Autumn 2023)
- Previous syllabus (applies from Autumn 2020)
- Previous syllabus (applies from Autumn 2019)
- Previous syllabus (applies from Autumn 2016)
- Previous syllabus (applies from Autumn 2013)
- Previous syllabus (applies from Autumn 2012, version 3)
- Previous syllabus (applies from Autumn 2012, version 2)
- Previous syllabus (applies from Autumn 2012, version 1)
- Previous syllabus (applies from Autumn 2010)
- Previous syllabus (applies from Autumn 2009)
- Previous syllabus (applies from Autumn 2008, version 2)
- Previous syllabus (applies from Autumn 2008, version 1)
- Previous syllabus (applies from Autumn 2007, version 2)
- Previous syllabus (applies from Autumn 2007, version 1)
Applies from: Autumn 2020
Some titles may be available electronically through the University library.
Proteins : biochemistry and biotechnology
Second edition: Chichester, West Sussex: Wiley Blackwell, 2014
Williamson, Michael P.
How proteins work
New York: Garland Science, c2012