Advanced Protein Science 1 - Protein Interactions and Sequences

Course content

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.

Education

MSc Programme in Biochemistry

Learning outcome

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.

Lectures, student presentations, group discussions and laboratory and computer exercises, written reports for evaluation.

See Absalon.

Bachelor degree either in biochemistry, nanotechnology, chemistry, or molecular biomedicine.

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.

ECTS
7,5 ECTS
Type of assessment
Oral examination, 20 min. (no preparation)
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Aid
Without aids
Marking scale
7-point grading scale
Censorship form
No external censorship
Several internal examiners
Criteria for exam assessment

In order to obtain the grade 12 the student should convincingly and accurately demonstrate the knowledge, skills and competencies described under "Learning Outcome".

 

Single subject courses (day)

  • Category
  • Hours
  • Exam
  • 0,5
  • Preparation
  • 143,5
  • Lectures
  • 14
  • Colloquia
  • 7
  • Practical exercises
  • 20
  • Theory exercises
  • 21
  • English
  • 206,0