Molecular Recognition in Biological Systems

15 credits

Syllabus, Master's level, 1KB454

A revised version of the syllabus is available.
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)
Finalised by
The Faculty Board of Science and Technology, 12 April 2013
Responsible department
Department of Chemistry - BMC

Entry requirements

120 credits in Science including 60 credits Chemistry, and at least Biochemistry, 20 credits thereof, or equivalent, or 120 credits in Science including Chemistry 30 credits and Biology 30 credits and at least Biochemistry 20 credits thereof, or equivalent.

Learning outcomes

After having completed the course the student are expected to 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
  • account for the concepts of affinity and selectivity based on stereochemical and thermodynamic principles
  • describe and discuss the dynamics and plasticity of proteins in relationship to molecular interactions, especially affinity and selectivity
  • use molecular graphics to study biomacromolecular structures and their complexes
  • list common biological, biochemical and biophysical methods for the study of molecular interactions and describe the principle of how they work and the information they can provide
  • account for molecular recognition of proteins, carbohydrates, nucleic acids and lipids by synthetic molecules
  • exemplify application of chemical compounds designed and synthesised to identify proteins and other biomacromolecules

Content

Molecular interaction mechanisms and forces between molecules, 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 and their properties can be described in terms of the molecular interactions involved. Application of molecular interaction analysis in life science research, drug discovery and diagnostics

Instruction

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

Assessment

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.

FOLLOW UPPSALA UNIVERSITY ON

facebook
instagram
twitter
youtube
linkedin