Ms. Leoni Oberbarnscheidt

Photo of Leoni  Oberbarnscheidt

Dr. Leoni Oberbarnscheidt

hat die Gruppe im April 2011 verlassen /
left the group: April 2011

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • B.Sc.(Biochemistry), 2005, Heinrich-Heine University, Düsseldorf, Germany

Second degree and/or intermediate examination:

  • MRes (Functional Genomics), 2007, University of York, York, United Kindom

Postgraduate degree

  • Dr. rer. nat. 2011, Heinrich Heine University, Duesseldorf, Germany

 

Publications:

  • Oberbarnscheidt L, Janissen R, Oesterhelt F. (2009); Direct and model free calculation of force-dependent dissociation rates from force spectroscopic data.; Biophys J.; 97(9):L19-21.
  • Oberbarnscheidt L, Janissen R, Martell S, Engelhard M, Oesterhelt F. (2009); Single-molecule force spectroscopy measures structural changes induced by light activation and transducer binding in sensory rhodopsin II.; J Mol Biol.; 394(3):383-90.
  • Cisneros DA, Oberbarnscheidt L, Pannier A, Klare JP, Helenius J, Engelhard M, Oesterhelt F, Muller DJ., 2008, Transducer binding establishes localized interactions to tune sensory rhodopsin II, Structure 16(8):1206-13
  • Janissen R, Oberbarnscheidt L, Oesterhelt F.(2009); Optimized straight forward procedure for covalent surface immobilization of different biomolecules for single molecule applications.; Colloids Surf B Biointerfaces; 71(2):200-7.
  • Cisneros DA, Oberbarnscheidt L, Pannier A, Klare JP, Helenius J, Engelhard M, Oesterhelt F, Muller DJ., 2008, Transducer binding establishes localized interactions to tune sensory rhodopsin II, Structure 16(8):1206-13
  • Oberbarnscheidt L, Taylor EJ, Davies GJ, Gloster TM, 2007; Structure of a carbohydrate esterase from Bacillus anthracis, Proteins. 66(1):250-2.

Attended conferences:

  • Trinational Fall Meeting GBM, Signal Transduction and Disease, Aachen, Germany, 2009 - Poster presentation: ‘Atomic force spectroscopy measures induced structural changes in Sensory Rhodopsin II’
  • Scanning Probe Microscopies and Organic Materials XVII, Bremen University, Bremen, Germany, 2009 - Oral presentation: ‘Atomic force spectroscopy measures induced structural changes in Sensory Rhodopsin II’
  • Biophysical Society 53rd Annual Meeting, Boston, USA, 2009 - Oral presentation: ‘Atomic force spectroscopy measures induced structural changes in Sensory Rhodopsin II’
  • Xth Annual Linz Winter Workshop, Linz University and Agilent, Linz, Austria, 2008 - Poster presentation: ‘Analysis of light acitvation and transducer binding of Sensory Rhodopsin II from Natromonas pharaonis by AFM’
  • IX. Annual Linz Winter Workshop, Linz University and Agilent, Linz, Austria, 2007 - Attended conference

Prices/Scholarships:

  • Poster prize of the study group Biophysics at the Trinational Fall Meeting GBM, Aachen, 2009
  • From 11/2008 to 07/2010: Full scholarship of the NRW-Research School BioStruct, Heinrich Heine University, Düsseldorf, Germany

BioStruct PhD project

Investigation of structure function relationship of membrane proteins using atomic force microscopy
The atomic force microscope is a powerful tool to learn about the intra- and intermolecular interactions of proteins. The focus of the project is on the investigation of membrane proteins by (I) AFM based unfolding and (II) protein-ligand force measurements. By unfolding, forces stabilizing sensory rhodopsin II from Natromonas pharaonis (NpSRII) are going to be measured under different conditions of biological relevance, i.e. alone as well as in complex with its transducer, both in the absence and presence of blue light. Whereas light activation in the presence of the transducer triggers a signalling cascade, which initiates the photophobic response of the bacterium, SRII acts as a proton pump in its absence. Changes in the forces of sensory rhodopsin II in the different conditions indicate differences in molecular interactions, which may lead to a further understanding of the molecular mechanism and recognition processes. In a second part, the lantibiotic nisin, which is covalently bound to the tip via a PEG-linker, is going to be presented to the functional ABC-transporter NisT embedded in an inside-out-vesicle. Here, the amount of force peaks in the retraction cycle and rate-dependant unfolding forces might give insights in the energy landscape of this ligand-receptor relationship.

Supervisors

Topic Supervisor:

undefinedProf. Dr. Filipp Oesterhelt, Institut für Physikalische Chemie II, Heinrich Heine Universität Düsseldorf, Oesterhelt Group

Complementary Supervisor:

undefinedProf. Dr. Lutz Schmitt, Institut für Biochemie, Heinrich Heine Universität Düsseldorf, Schmitt Group

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