Syllabus for Protein Engineering

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: Biology A1F, Technology A1F, Applied Biotechnology A1F, Chemistry 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:

    First cycle

    • 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

    Second cycle

    • 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: The Faculty Board of Science and Technology
  • Revised: 2012-05-25
  • Revised by: The Faculty Board of Science and Technology
  • Applies from: Autumn 2012
  • Entry requirements:

    150 credits including Molecular Cell Biology, Functional Genomics, Molecular Infection Biology or Genome Biology. Alternatively 30 credits within the Master programme in Applied Biotechnology, Molecular Biotechnology or Chemistry with specialisation in biochemistry.

  • Responsible department: Biology Education Centre

Learning outcomes

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. After completing 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 lab journal according to 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. Production of modified products.

The student will also propose solutions to biotechnical problems, and document their own laboratory activities, which is aimed to prepare them for the demands of their future employment.


The course consists of lectures, guest lectures, seminars, group work and laboratory sessions. Participation in seminars, laboratory sessions and connected lectures, group work, tests and computer exercises is compulsory.


Theory part (7 credits):

Written examination that includes biotechnological methods, protein physical methods, and the structure and classification of proteins.

Practical part:

The student will submit a correctly kept laboratory journal, and report the results obtained in the laboratory (5 credits), as well as present a simple research plan (3 credits).

Reading list

Reading list

Applies from: Autumn 2012

Some titles may be available electronically through the University library.

  • Williamson, Michael P. How proteins work

    New York: Garland Science, c2012


    Find in the library