Syllabus academic year 2008/2009
(Created 2008-07-17.)

Higher education credits: 7,5. Grading scale: TH. Level: A (Second level). Language of instruction: The course will be given in English on demand. Alternative for: MLIV1. Optional for: B4l, B4mb, B4pt, K4l. Course coordinator: Prof Bertil Halle, och prof Sara Linse,, Biofysikalisk kemi. Recommended prerequisits: Basic physical chemistry, at a level comparable to the LTH courses KFK080 Thermodynamics and KFK090 Molecular interactions and dynamics. Assessment: The final grade is based on weekly take-home problem assignments (67%) and a written midterm exam (33%). Laboratory practicals and oral presentation must be completed. If necessary, reexamination (of the midterm exam) will be performed orally. Further information: The course emphasizes active processing of knowledge through take-home problem assignments and laboratory practicals. The course ends with a “mini symposium”, where the students present and critically discuss current research problems in protein science. Home page:

The course aims at giving the student:

Knowledge and understanding
For a passing grade the student must

Skills and abilities
For a passing grade the student must

Judgement and approach
For a passing grade the student must

The course addresses the following main topics:

The chemical building-blocks and three-dimensional structures of proteins: Structure analysis by X-ray crystallography; Structure and sequence databases.

Protein characterization by optical spectroscopy: Physical principles and applications of fluorescence and circular dichroism spectroscopy.

Polypeptide conformation: Models of polymer conformation and conformational transitions; Conformational entropy; Folding cooperativity.

Protein energetics and stability: Packing; Hydration; Electrostatics; Thermal and solvent-induced denaturation; Differential scanning calorimetry.

Protein dynamics: Kinetic models; Proton exchange; Diffusion control; Protein folding; Motor proteins; Computer simulation of proteins.

Nuclear magnetic resonance: Principles of NMR spectroscopy and relaxation; Analysis of structure, interactions and dynamics of proteins in solution.

Association processes: Ligand binding; Allostery; Protein aggregation; Isothermal titration calorimetry; Surface plasmon resonance.

The course literature consists of a compendium in Molecular Protein Science, written by the teachers on the course, and of manuals for the practicals. For those who want go deeper, the course website offers a list of selected references and links to the literature.