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Expertise in Structural Biology

Solid-State NMR Spectroscopy

Solid-State NMR Spectroscopy is emerging as a powerful tool for structural investigations on biological macromolecules which are not amenable to the standard techniques as solution NMR spectroscopy or X-ray crystallography. In contrast to solution NMR spectroscopy, solubility is not a prerequisite for systems to be studied by solid-state NMR spectroscopy, and for molecular complexes, no upper limit for the molecular weight exists. Thus, solid-state NMR spectroscopy has proven its power for the study of structure and dynamics of membrane proteins, membrane protein complexes and amorphous and fibrillar protein aggregates. With the help of special techniques, it is possible to select only parts of the protein by their mobility or by their vicinity to highly mobile entities as water molecules or the inner part of a membrane double layer, and study them individually. Thus, this technique can give important insight into the overall organisation and the topology of membrane proteins as well as into molecular interactions in systems which are not readily crystallisable.

Figure Legend:
A: Rotor Containing the Immobilized Sample
B: The Sample is Spun around an Axis Inclined by 54.7° with Respect to the Magnetic Field
C: Probe Head
D: Magnet

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