Molecular Recognition in Biological Systems

15 credits

Syllabus, Master's level, 1KB454

A revised version of the syllabus is available.
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)
Finalised by
The Faculty Board of Science and Technology, 13 March 2008
Responsible department
Department of Chemistry - BMC

Entry requirements

120 credits in Science including 60 credits Chemistry, and at least Biochemistry, 10 credits thereof, or equivalent.

Learning outcomes

After having completed the course the student should be able to:

  • describe and discuss forces and interactions between biomacromolecules and between small molecules and biomacromolecules in thermodynamic terms.
  • describe and discuss the concepts affinity and selectivity in stereochemical and thermodynamic terms.
  • describe and discuss the underlying principles of molecular recognition based on three-dimensional structures of biomacromolecules complexed with other biomacromolecules or small molecule ligands
  • describe and discuss the relationship between dynamics and plasticity of proteins and molecular interactions as well as consequences of dynamics and plasticity for affinity and selectivity.
  • use molecular graphics to study biomacromolecular structure and structures of biomacromolecular complexes
  • describe and discuss molecular recognition of proteins, carbohydrates, nucleic acids and lipids by synthetic molecules
  • describe and discuss fields of use of chemical compounds designed and prepared for the purpose of recognizing and binding proteins and other biomacromolecules.


Forces between molecules, selectivity and affinity, multivalency, avidity, entropy and its role in molecular recognition, structure and dynamics of biomacromolecules and their complexes, stereochemistry and complexation, protein-protein interactions, DNA-protein interactions, RNA-protein interactions, inhibition of protein-protein interactions, protein plasticity, design of high-affinity binders for biomacromolecules their complexes and domains, kinetics and molecular interactions, methods for the study of strong and weak interactions, molecular graphics and structural information, examples from molecular interactions in vivo and in vitro.


Lectures, exercises, laboratory work and discussions. Training in oral and written reports


Written exams are offered at the end of the course and/or during the course, corresponding to 10 credits. Experimental work corresponds to 5 credits. To pass the course the student must pass both the theoretical and the experimental parts. The final grade is the weighted grade of both theoretical and experimental work.