Course syllabus

Biofysikalisk kemi
Biophysical Chemistry

KFK032, 7,5 credits, A (Second Cycle)

Valid for: 2012/13
Decided by: Education Board 2
Date of Decision: 2012-04-04

General Information

Main field: Biotechnology.
Elective for: B4-l, B4-mb, B4-pt, K4-l
Language of instruction: The course will be given in English on demand

Aim

The course aims at giving the student:

• molecular-level understanding of the structure, stability, interactions and dynamics of proteins
• knowledge about the principal physical methods used in modern protein science
• practical experience in using some of these methods
• the knowledge base needed to use and critically assess the protein research literature

Learning outcomes

Knowledge and understanding
For a passing grade the student must

• describe the principal physico-chemical properties of proteins, such as structure, stability, interactions and dynamics
• account for these properties in terms of molecular-level theroetical models
• interpret experimental results from physico-chemical studies of proteins

Competences and skills
For a passing grade the student must

• use physico-chemical concepts and models to solve problems involving proteins
• apply his/her theoretical knowledge to biotechnological and biomedical problems
• use electronic protein data bases
• carry out spectroscopic measurements on proteins

Judgement and approach
For a passing grade the student must

• read and critically assess the research literature in protein science
• communicate effectively with researchers in protein science

Contents

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.

Examination details

Grading scale: TH
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.

Admission

Admission requirements:

• KFK080 Thermodynamics or KFKA05 Molecular Driving Forces 1: Thermodynamics
• KFK090 Molecular Interactions and Dynamics or KFKF01 Molecular Driving Forces 2: Interactions and Dynamics

The number of participants is limited to: No

Reading list

• 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.

Contact and other information

Course coordinator: prof Bertil Halle, bertil.halle@bpc.lu.se
Course homepage: http://www.cmps.lu.se/bpc/teaching/
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.