Ms. Katherina Hemmen

 

 

 

 

 

 

 

Katherina Hemmen M.Sc.

Seidel Group
Physikalische Chemie II
Heinrich Heine University
Universitätsstr.1
Building: 26.42
Floor/Room: 02.29
40225 Düsseldorf
Phone +49 211 81-14862
Fax +49 211 81-13569

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • B. Sc. Biotechnology, 2010, University of Applied Sciences Emden/Leer, Emden, Germany

Second degree and/or intermediate examination:

  • M. Sc. Biotechnology, 2012, Technical University Carolo Wilhelmina of Braunschweig, Braunschweig, Germany

Publications:

  • Hemmen, K., Reinl, T., Buttler, K., Behler, F., Dieken, H., Jänsch, L., Wilting, J., et al. (2011). High-resolution mass spectrometric analysis of the secretome from mouse lung endothelial progenitor cells. Angiogenesis, 14(2), 163-172.
  • Badar, M., Hemmen, K., Nimtz, M., Stieve, M., Stiesch, M., Lenarz, T., Hauser, H., et al. (2010). Evaluation of madurahydroxylactone as a slow release antibacterial implant coating. The open biomedical engineering journal, 4(i), 263-270.

BioStruct PhD project

Phage T4 lysozyme is an endoacetyl muramidase which is produced late in the infection phase of E. coli. It is a model enzyme which has been used for structural studies already more than 30 y ago. It was observed that the substrate-free as well as the substrate-bound form crystallizes in the same conformation, although in the substrate-free form the catalytic cleft is blocked by a salt bridge. Thus, in order for the substrate to enter the cleft, the T4L has to undergo an opening motion which occurs over α helix 3. The details of this motion will be explored in further detail with smFRET measurements. Syntaxin 1 A belongs to the family of SNARE proteins, which are responsible for synaptic vesicle release. Syntaxin 1 A exists in at least two different conformations, a “closed” state in which all four helices are packed together and an “open” state in which the H3 helix in turned away from the three Habc helices. This state exists in the SNARE complex formed by syntaxin 1A, SNAP25 and synaptobrevin. However, recent measurements indicated the existence of further motion in the Habc-domain which will be explored using smFRET and NMR measurements.

Supervisors

Topic Supervisor:

undefinedProf. Dr. C. Seidel, Institute for physical chemistry, Seidel Group

Second Supervisor:

undefinedProf. Dr. D. Willbold, Institute for physical biology, Willbold Group

Responsible for the content: E-MailBioStruct Office