NBIK10023U Advanced Protein Science 1 - Protein Interactions and Sequences

Volume 2013/2014
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.
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.



Competencies:
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.




Literature
See Absalon.
Bachelor degree either in biochemistry, nanotechnology, chemistry, or molecular biomedicine. Other applicants may be admitted on the basis of an evaluation of their individual qualifications. Basic knowledge of protein science is a requirement.
Lectures, student presentations, group discussions and laboratory and computer exercises, written reports for evaluation.
  • Category
  • Hours
  • Colloquia
  • 7
  • Exam
  • 0,5
  • Lectures
  • 14
  • Practical exercises
  • 20
  • Preparation
  • 143,5
  • Theory exercises
  • 21
  • Total
  • 206,0
Credit
7,5 ECTS
Type of assessment
Oral examination, 20 minutes
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Marking scale
7-point grading scale
Censorship form
No external censorship
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.