The course provides an overview of experimental methods for the determination of structures of macromolecules at atomic resolution.
Learning objective
Insight into the methodology, areas of application and limitations of two principal methods for the structure determination of biological macromolecules.
Content
Part I: Methods for the determination of the structure of proteins and macromolecular complexes using X-ray diffraction in single crystals. Part II: Methods for the determination of protein structures in solution using nuclear magnetic resonance (NMR) spectroscopy. Experimental approaches to the characterization of intramolecular dynamics of proteins.
Literature
1) Wüthrich, K. NMR of Proteins and Nucleic Acids, Wiley-Interscience. 2) Blow, D. Outline of Crystallography for Biologists. Oxford University Press.
Performance assessment
Performance assessment information (valid until the course unit is held again)
The performance assessment is offered every session. Repetition possible without re-enrolling for the course unit.
Mode of examination
written 90 minutes
Additional information on mode of examination
Examination in 2 parts. Duration of X-ray part 45 Min. Duration of NMR part 45 Min. Die Prüfung besteht aus zwei Teilen: 45 Min. für X-ray und 45 Min. für NMR
Written aids
Keine Hilfsmittel zugelassen.
This information can be updated until the beginning of the semester; information on the examination timetable is binding.
Learning materials
No public learning materials available.
Only public learning materials are listed.
Groups
No information on groups available.
Restrictions
There are no additional restrictions for the registration.
Performance assessment as a semester course