Syllabus for Molecular Recognition in Biological Systems

Molekylär igenkänning i biologiska system

  • 15 credits
  • Course code: 1KB454
  • Education cycle: Second cycle
  • Main field(s) of study and in-depth level: Biology A1N, Chemistry A1N
  • Grading system: Fail (U), Pass (3), Pass with credit (4), Pass with distinction (5)
  • Established: 2008-03-13
  • Established by:
  • Revised: 2018-08-30
  • Revised by: The Faculty Board of Science and Technology
  • Applies from: week 24, 2019
  • Entry requirements: 120 credits in Science including 60 credits Chemistry, and at least Biochemistry, 20 credits thereof, or 120 credits in Science including Chemistry 30 credits and Biology 30 credits, and at least Biochemistry 20 credits thereof.
    English language proficiency that corresponds to English studies at upper secondary (high school) level in Sweden ("English 6").
  • Responsible department: Department of Chemistry - BMC

Learning outcomes

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

  • describe and discuss the molecular recognition of biomacromolecules (proteins, carbohydrates, nucleic acids) and other biomolecules and small synthetic molecules.
  • explain basic principles of molecular recognition based on kinetic and thermodynamic principles, and the three-dimensional structures of biomacromolecules in complex with other molecules
  • use molecular graphics to study biomacromolecular structures and their complexes
  • compare common biological, biochemical and biophysical methods for the study of molecular interactions in terms of how they work and the information they can provide
  • exemplify application of chemical compounds designed and synthesised to identify proteins and other biomacromolecules


Molecular interaction mechanisms and forces between molecules: selectivity, affinity, kinetics and thermodynamics. The effect of the environment on interactions.
Structure and dynamics of biomacromolecules and their complexes: selectivity, multivalency, avidity. Various types of biomolecular interactions: protein-ligand, protein-protein , DNA-protein , RNA-protein. Inhibition of interactions.
Applications: design of ligands, modification of proteins and nucleic acids to alter their interactions with other macromolecules or ligands.
Biological, biochemical and biophysical methods for the identification and characterisation of molecular interactions.
Modelling of interactions by molecular graphics and structural information.
Examples of how biological systems can be described in terms of the molecular interactions involved. Application of molecular interaction analysis in life science research, drug discovery and diagnostics


Lectures, tutorials, laboratory work and projects. Tutorials, laboratory work and projects are compulsory and are performed individually.


A written examination is organised at the end of the course (10 credits). Laboratory work, exercises and projects are examined during the course and are equivalent to 5 credits. The final grade is given as a weighted average of the written examination and the other examined components.

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.

Reading list

The reading list is missing. For further information, please contact the responsible department.