Biophysics

• Introduction into the physical principles of protein function in trnacription, RNA interactions, membrane transport and signal transduction,
• NMR to understand structure and dynamics of proteins
• High-pressure NMR to investigate the conformational landscape of proteins
• High-resolution structures by X-ray diffraction and crystallography
• Time-resolved structures by free electron laser
• Single particle analysis and cryo-electron microscopy
• Homology modelling and structure modelling
• Electron-Tomography, Scanning electron microscopy and correlative light-and electron microscopy
• FRET and TIRD microscopy
• Presentation and discussion of a research based topic in the field of structural biology with a focus on the methods discussed in the lecture: NMR, X-ray, EM, FRET

1. at least two lectures from the following (WS and SS):

• Structural Biology I & II or
• Physical Biochemistry I & II

2. one seminar from the following (WS and SS):

• Structural Biology I & II or
• Physical Biochemistry I & II

In the seminar a seminar presentation has to be held and registered in Flexnow as an ungraded study achievement (Studienleistung).

Note! If you are not sure what lectures and seminar to select, please contact the person in charge of the module.
The selection may depend on the examiner you choose for the module examination.

30 min oral examination (graded)

Examiner:

• Prof. Dr. Remco Sprangers
• Prof. Dr. Christine Ziegler
• Prof. Till Rudack

The student can choose the examiner.

Please get in contact with the examiner of your choice to arrange a date of the oral examination, than register the examination in flexnow.

• Expression and purification of membrane proteins
• Single Particle Data collection and electron microscopy
• Two-dimensional and three-dimensional membrane protein crystallization
• Introduction into EM and X-ray data analysis
• Homology modelling as tool for structure determination at low resolution
• Presentation and discussion of own experimental gained data

• Expression and purification of NMR isotope labelled proteins
• Collection of 1 and 2 dimensional NMR experiments
• Analysis of multidimensional NMR spectra
• Collection and analysis of NMR data to assess protein dynamics
• Performance of NMR titration data to extract binding characteristics
• Shift of the conformational equilibrium using high pressure NMR
• Presentation and discussion of own experimental gained data