Molecules of Life I

A. Baumann (Forschungszentrum Jülich, Cellular Biophysics)
R. Merkel (Forschungszentrum Jülich, Biomechanics)
J. Fitter (Forschungszentrum Jülich, Molecular Biophysics)
C. Seidel (Uni Düsseldorf, Molecular Physical Chemistry )
B. König (Forschungszentrum Jülich, Structural Biochemistry)
J. Granzin (Forschungszentrum Jülich, Molecular Biophysics)
O. H. Weiergräber (Forschungszentrum Jülich, Molecular Biophysics)
coordinated by J. Fitter (Forschungszentrum Jülich, Molecular Biophysics)
(building 15.1X, room 249)

The lecture series "Molecules of Life I" provides an introduction to biological molecules as well as the techniques to study them. For each topic, there will be a different lecturer who will introduce the molecules as well as the technique in a 2-hour lecture. With some previous knowledge about the topic, it should be possible to listen to single lectures or the series.

• Wednesday, October 7, 3:00-4:30 (room change: building 04.8, IFF lecture hall)
  A. Baumann (Cellular Biophysics)
  Components of the cell: an introduction to cellular function
• Wednesday, October 28, 1:00-2:30
  R. Merkel (Biomechanics)
  Biomembranes - Biomimetics and Real Live
  • concepts: lipid molecules, membrane proteins, fluid mosaic model
  • techniques: model membranes, supported bilayers, fluorescence recovery after photobleaching and single particle tracking for mobility analysis of membrane molecules, micropipette aspiration for membrane mechanical studies
• Wednesday, November 18, 3:00-4:30
  J. Fitter (Molecular Biophysics)
  How proteins get folded and how they stay folded
  • early experiments on protein folding: Mirsky's, Neurath's and Anfinsen's findings
  • concepts and models of protein folding: transition state theory; two-state and multi state models; intermediate states; folding funnels and energy landscapes
  • thermodynamics and kinetics of protein folding: equilibrium and non-equilibrium transitions; protein stability in extremophiles and mesophiles
  • classical techniques in protein folding: differential scanning calorimetry; fluorescence and CD spectroscopy
  • the perspectives of single molecule techniques in protein folding: some short examples
  • towards protein folding in the cell: co-translational folding versus refolding; folding, misfolding, and aggregation in crowed environments; misfolding diseases
• Wednesday, December 9, 3:00-4:30
  C. Seidel (Molecular Physical Chemistry, Uni Düsseldorf)
  Structure and dynamics of RNA and DNA
• Wednesday, January 20, 3:00-4:30
  B. König (Structural Biochemistry)
  Protein structure and protein/ligand interactions, insight from liquid state NMR spectroscopy

  Basic principles of NMR spectroscopy, NMR observables, and interactions between nuclear spins will be introduced. The strategy of protein structure determination by solution NMR will be discussed. NMR-based approaches for investigation of protein-ligand interactions will be presented. The potential of NMR spectroscopy in life science will be illustrated by research results from ISB-3.

• Wednesday, February 10, 3:00-4:30 (room change: building 16.13, seminar room)
  J. Granzin and O. H. Weiergräber
  Proteincrystallography, Protein-Protein Complexes and Signal Transduction
  
  Quality evaluation of protein structures from the PDB (x-ray and nmr; resolution, conformation...classification), type of folding and structural motif, methods to investigate protein-protein interactions, practical examples visualised with a graphics program.