NBIK10023U Advanced Protein Science 1 - Protein Interactions and Sequences
The course is an introduction to biophysical techniques used in
protein science to measure structural and biophysical properties of
proteins. It includes the biophysical methods of optical
spectroscopy (circular dichroism, fluorescence, absorbance), mass
spectrometry, surface plasmon resonance, isothermal and
differential scanning calorimetry, NMR spectroscopy, and small
angle x-ray scattering.
The focus is on the theoretical background of the methods, the
instrumentation, and on the application of these methods in protein
science. The course is a mixture of lectures and group discussions
of fundamental topics in each of the methodologies, and for most of
these hands on introduction to both the experimental and analytical
tools of these methods.
Teaching Tuesdays and Thursday mornings + hands-on
exercises.
To use the knowledge of the principles of the presented
biophysical in evaluations of their application to protein science
research projects.
Knowledge:
Knowledge on advanced protein biophysics techniques and
instrumentation regarding optical spectroscopy (circular dichroism,
fluorescence, absorbance), mass spectrometry, surface plasmon
resonance, isothermal and differential scanning calorimetry, NMR
spectroscopy, and small angle x-ray scattering.
Skills:
The student will be able to design, execute and present experiments
in advanced protein biophysics regarding optical spectroscopy
(circular dichroism, fluorescence, absorbance), mass spectrometry,
surface plasmon resonance, isothermal and differential scanning
calorimetry, NMR spectroscopy, and small angle x-ray scattering.
Competences:
Critically evaluate data obtained in advanced protein biophysics
regarding optical spectroscopy (circular dichroism, fluorescence,
absorbance), mass spectrometry, surface plasmon resonance,
isothermal and differential scanning calorimetry, NMR spectroscopy,
and small angle x-ray scattering.
See Absalon.
- Category
- Hours
- Colloquia
- 7
- Exam
- 0,5
- Lectures
- 14
- Practical exercises
- 20
- Preparation
- 143,5
- Theory exercises
- 21
- Total
- 206,0
As
an exchange, guest and credit student - click here!
Continuing Education - click here!
- Credit
- 7,5 ECTS
- Type of assessment
- Oral examination, 20 minutes---
- Marking scale
- 7-point grading scale
- Censorship form
- No external censorship
Several internal examiners
Criteria for exam assesment
In order to obtain the grade 12 the student should convincingly
and accurately demonstrate the knowledge, skills and competencies
described under "Learning Outcome".
In order to pass the course the students must have performed the
following at a satisfactory level:
- Performed a supervised practical project including designing and executing an experiment, using one of the selected methods of the course.
- Written one report covering the performed experiment. The report should cover: 1) description and critical evaluation of the method; 2) explanation of typical protocols and strategies used; 3) data evaluation; 4) presentation of the results including graphs, analyses, and calculated results; 5) a critical analysis of the results; 6) estimation of experimental errors and an explanation of these.
Course information
- Language
- English
- Course code
- NBIK10023U
- Credit
- 7,5 ECTS
- Level
- Full Degree Master
- Duration
- 1 block
- Placement
- Block 3
- Schedule
- A
- Course capacity
- 25 students
Priority will be given to biochemistry students - Continuing and further education
- Study board
- Study Board of Biomolecular Sciences and Technology
Contracting department
- Department of Biology
Course responsibles
- Birthe Brandt Kragelund (bbk@bio.ku.dk)