| TFKE37 |
Biological Measurements, 6 ECTS credits.
/Biomätteknik/
For:
KeBi
PRO
|
OBS! |
Canâ?Tt be combined with other courses Ht1 due to special scheduling
|
| |
Prel. scheduled
hours: 48
Rec. self-study hours: 112
|
| |
Area of Education: Technology
Main field of studies: Chemical biology
|
| |
Advancement level
(G1, G2, A): G2
|
|
Aim:
The objectives of the course is to provide comprehensive knowledge in the following areas: Measurable properties of biomolecules, light spectroscopy, nuclear magnetic resonance, calorimetry, surface plasmon resonance, fundamental principles for separation based on macromolecular mobility in centrifugal- and electrical force fields as well as direct forces. Furthermore, comprehensive knowledge will be provided regarding applications of these methods within clinical and biomedical analysis, both functional and qualitative. After studies well learned the student will have proficiency to:
- Understand and explain the theory behind the methods that are explained in the course.
- Describe areas of application as well as advantages and limitations with the different methods.
- Analyze, evaluate and draw conclusions from results obtained with the methods treated in the course.
- Propose methods and strategies for studies of specific questions within biochemical and biomedical analysis, and communicate these proposals in novel contexts.
- Investigate laboratory techniques and practice some of the methods treated in the course.
|
|
Prerequisites: (valid for students admitted to programmes within which the course is offered)
Biokemi 2 (or similar), Physical Chemistry
Note: Admission requirements for non-programme students usually also include admission requirements for the programme and threshhold requirements for progression within the programme, or corresponding.
|
|
Organisation:
Lectures, seminars and laboratory exercises.
|
|
Course contents:
Different optical methods for the study of biological systems, such as UV, IR, FT-IR, circular dichroism (CD) and fluorescence spectroscopy, calorimetric methods, surface plasmon resonance (SPR), and the fundamental principles for separation by macromolecular mobility in centrifugal and electrical fields, such as electrophoresis, sedimentation analysis and mass spectrometry. The laboratory exercises will include practice or demonstration of a majority of the techniques treated in the lecture course.
|
|
Course literature:
Compendium with extracts from reference literature, reviews, scientific articles and laboratory handouts. The reference literature includes:
Biophysical Chemistry part II. Cantor & Schimmel, Freeman NY 1980.
Principles of Physical Biochemistry. VanHolde, Johnsson & Ho. Prentice Hall 1998.
Principles and techniques of practical biochemistry. Wilson & Walker, Cambridge University Press 2000.
Protein-Ligand Interactions: hydrodynamics and calorimetry samt Protein-Ligand Interactions: structure and spectroscopy, Harding & Chowdry, Oxford University Press 2001.
|
|
Examination: |
|
A written examination
A laboratory course including literature projekt
|
4,5 ECTS
1,5 ECTS
|
| |
|
|
Course language is English.
Department offering the course: IFM.
Director of Studies: Magdalena Svensson
Examiner: Maria Sunnerhagen
Course Syllabus in Swedish
|
|