|
Our
group focuses on the preparation of membrane polypeptides and their
investigation by NMR spectroscopic methods. Whereas the well
established solution NMR techniques are applied to define the secondary
structure of polypeptides in the presence of detergent micelles,
solid-state NMR techniques are required to investigate the structure,
topology, dynamics and interactions of these proteins when associated
with phospholipid bilayers. Our goal is to establish structure-function
relationships and to correlate the primary sequence information of
membrane-associated polypeptides with structural features. The
structural investigation of polypeptides by solid-state NMR
spectroscopy requires the uniaxial orientation of the membrane systems,
or fast spinning around the so called `magic angle'. The former can be
achieved by mechanical alignment of the bilayers along glass surfaces
or by magnetic orientation of the membranes in the field of the NMR
spectrometer. The mechanical alignment of
bilayers works best when flat-coil NMR probe heads are available. These
are built from scratch in our group with the help of electronic
analytical equipment.
|
