NBIK22002U Advanced Protein Science 1 - Biophysical Methods
MSc Programme in Biochemistry
MSc Programme in Physics
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,incl single molecule
fluorescence, absorbance), hydrogen exchange 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, one
exercise pr student.
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), hydrogen exchange mass spectrometry, surface plasmon
resonance, isothermal and differential scanning calorimetry, NMR
spectroscopy, and small angle x-ray scattering.
See Absalon.
It is necessary that a basic course in protein science has been passed. It is an advantage that the student has passed Protein Science A or C, or the protein research lab.
- Category
- Hours
- Lectures
- 14
- Class Instruction
- 7
- Preparation
- 143,5
- Theory exercises
- 21
- Practical exercises
- 20
- Exam
- 0,5
- Total
- 206,0
Oral feedback both individually and in groups on oral presentations. Oral and written feedback on the laboratory report and presentation.
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Continuing Education - click here!
- Credit
- 7,5 ECTS
- Type of assessment
- Oral examination, 20 min. (no preparation)
- Type of assessment details
- ---
- Exam registration requirements
In order to be admitted to the exam 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.
- Aid
- Without aids
- Marking scale
- 7-point grading scale
- Censorship form
- No external censorship
Several internal examiners
- Re-exam
The same as the ordinary exam.
If the requirement of a supervised practical project including designing and executing an experiment, using one of the selected methods of the course, has not been fulfilled, the student will need to take the course again.
If the requirement of a written report has not been fulfilled, it can be fulfilled no later than three weeks before the reexamination by agreement with the course responsible.
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".
Course information
- Language
- English
- Course code
- NBIK22002U
- Credit
- 7,5 ECTS
- Level
- Full Degree Master
- Duration
- 1 block
- Placement
- Block 3
- Schedule
- A
- Course capacity
- 28
The number of places might be reduced if you register in the late-registration period (BSc and MSc) or as a credit or single subject student.
Study board
- Study Board for the Biological Area
Contracting departments
- Department of Biology
- Department of Pharmacy
- Department of Chemistry
- The Niels Bohr Institute
Contracting faculty
- Faculty of Science
Course Coordinators
- Birthe Brandt Kragelund (bbk@bio.ku.dk)