Valid from: Autumn 2017
Decided by: Margareta Sandahl
Date of establishment: 2017-05-15
Division: Biophysical Chemistry
Course type: Course given jointly for second and third cycle
The course is also given at second-cycle level with course code: KFKN10
Teaching language: English
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
Knowledge and Understanding
For a passing grade the doctoral student must
Competences and Skills
For a passing grade the doctoral student must
Judgement and Approach
For a passing grade the doctoral student must
- The chemical building-blocks and three-dimensional structures of proteins: Structure analysis by X-ray crystallography; Structure and sequence databases; Bioinformatics. - 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; 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 the compendium "Biophysical Chemistry", authored and updated each year by the course teachers, and of manuals for the practicals. For those who want go deeper, the compendium provides a list of selected references and links to the literature.
Types of instruction: Lectures, seminars, laboratory exercises, project, study visit
Examination formats: Written exam, seminars given by participants
Grading scale: Failed, pass
Examiner:
Assumed prior knowledge: Under graduate courses in physical chemistry or physics including thermodynamics, intermolecular interactions and molecular dynamics.
Course coordinator: Kristofer Modig <kristofer.modig@lth.lu.se>
Web page: http://www.cmps.lu.se/bpc/education/kfk032/