Course syllabus
Biofysikalisk kemi
Biophysical Chemistry
KFKN10, 7,5 credits, A (Second Cycle)
Valid for: 2023/24
Faculty: Faculty of Engineering, LTH
Decided by: PLED B/K
Date of Decision: 2023-04-18
General Information
Main field: Biotechnology.
Main field: Pharmaceutical Technology.
Elective Compulsory for: MLAK1
Elective for: B4-l, B4-mb, K4-l, MBIO1, N4, N4-nbm
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 databases.
- carry out spectroscopic measurements on proteins.
Judgement and approach
For a passing grade the student must
- read and critically assess 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; 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.
Examination details
Grading scale: TH - (U,3,4,5) - (Fail, Three, Four, Five)
Assessment: The final grade is based on weekly take-home problem assignments (50%) and a written midterm exam (50%). Approved laboratory practicals and oral presentation are needed for a passing grade. If necessary, reexamination (of the midterm exam) will be performed orally.
The examiner, in consultation with Disability Support Services, may deviate from the regular form of examination in order to provide a permanently disabled student with a form of examination equivalent to that of a student without a disability.
Admission
Admission requirements:
- FAFA05 Physics - Waves, Thermodynamics and Atomic Physics or KFKA05 Molecular Driving Forces 1: Thermodynamics
- KOKA30 General, Inorganic and Organic Chemistry or KOOA15 General Chemistry
Assumed prior knowledge: KFKF01 Molecular Driving Forces 2: Interactions and Dynamics
The number of participants is limited to: No
The course overlaps following course/s: KFK032
Reading list
- 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.
Contact and other information
Teacher: Kristofer Modig, kristofer.modig@bpc.lu.se
Course coordinator: Kristine Steen Jensen, kristine_steen.jensen@bpc.lu.se
Course homepage: https://www.cmps.lu.se/education/
Further information: The course emphasizes active processing of knowledge through take-home problem assignments and laboratory practicals. Five lectures are devoted to research in protein science, where the students present and critically discuss recent research results.