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, 20 April 2012
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 are expected to be able to:

  • describe and discuss the kinetic and thermodynamic principles of the forces and interactions between biomacromolecules and between small molecules and biomacromolecules
  • describe and discuss the stereochemical and thermodynamic principles of affinity and selectivity
  • describe and discuss the underlying principles of molecular recognition based on three-dimensional structures of biomacromolecules in complex with other biomacromolecules or small molecule ligands
  • describe and discuss the dynamics and plasticity of proteins in relationship to molecular interaction, especially with respect to affinity and selectivity
  • use molecular graphics to study biomacromolecular structures and their complexes
  • describe and discuss molecular recognition of proteins, carbohydrates, nucleic acids and lipids by synthetic molecules
  • describe and discuss the use of chemical compounds designed and synthesised for recognition of proteins and other biomacromolecules


Forces between molecules, selectivity and affinity.

Entropy and its role in molecular recognition, multivalency, avidity.

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.

Interactions between low molecular weight compounds and proteins: Design of high-affinity binders for biomacromolecules, their complexes and domains. Kinetics and molecular interactions, methods for studies of strong and weak interactions.

Molecular graphics and structural information. Examples from molecular interactions in vivo and in vitro.

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.


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.