Protein Science

15 credits

Syllabus, Bachelor's level, 1KB433

Education cycle
First cycle
Main field(s) of study and in-depth level
Biology G2F, Chemistry G2F
Grading system
Fail (U), Pass (3), Pass with credit (4), Pass with distinction (5)
Finalised by
The Faculty Board of Science and Technology, 7 February 2023
Responsible department
Department of Chemistry - BMC

Entry requirements

One of the following is required: (1) 60 credits of which at least 40 credits in chemistry including 15 credits in biochemistry, or (2) 60 credits of which at least 40 credits in biology, and 15 credits in biochemistry.

Learning outcomes

On completion of the course, the student should be able to:

  • describe and compare biological mechanisms of peptide/protein synthesis and degradation,
  • describe the different levels of protein structure and the principles of protein folding and interaction with other molecules,
  • describe compare and apply methods as well as design strategies for the production, isolation and modification of proteins, and the determination of their physico-chemical, structural and functional properties,
  • explain the fundamental relationships between the properties of proteins and their biological funtions including their implication in various pathologies,
  • analyse and interpret protein sequences and structures and use such information to predict the properties of proteins,
  • describe how proteins can be used as drugs and for various industrial and scientific purposes,
  • explain the fundamental molecular mechanisms of drugs targeting proteins and the principle for development of such drugs,
  • communicate the use of proteins in research and common applications of proteins, via oral presentations and scientific posters.


Production and degradation: Biological and recombinant protein synthesis. Biological and chemical peptide synthesis. Post-translational and chemical modifications. Genetic engineering and targeted evolution. Protein degradation. Protein evolution.

Protein structure, function and bioinformatics: Protein folding and structural determination. Analysis of protein structure using molecular graphics. Protein interactions. Examples of proteins: enzymes, membrane proteins, structural proteins, DNA-binding regulatory proteins. Structure-function relationships. Introduction to databases for protein sequences, structures and functions. Protein bioinformatics tools and methods.

Applications: Use of proteins in biotechnological and medical research and development. Importance of proteins in the development of different types of drugs. Drug development strategies.

Practical and theoretical lab projects: Biotechnological and biochemical techniques to produce and characterize an enzyme. Protein crystallization.

Studies of how a given drug works at the biochemical level.


Lectures, laboratory work, theoretical exercises and project. Exercises and project are performed individually or in group.


Experimental and theoretical exercises and project (7 credits) during the course. A final written exam (8 credits) is given at the end of the course. 

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.

Other directives

Cannot be included in a degree together with the course Structure and funciton of proteins (1KB403, 1KB422) and Proteins and drugs (1KB404, 1KB423).