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In the general excitement of a time when three-dimensional protein
structures of whole genomes are being determined automatically, it is
often forgotten that a structure in itself does not tell one how the
molecule works or folds. For that, one needs to know a great deal about
mechanism, intermediates, structural dynamics and molecular
interactions. We gather this information using a wide range of
biochemical and biophysical techniques, including molecular biology,
transient kinetics and crystallography, mass spectrometry, and
computation, to understand the "jigglings and wigglings of atoms" in
model systems. We study mRNA processing, chaperone-assisted and
unassisted protein folding, and reactions that make use of flavin or
heme cofactors. In addition, we are part of the Advanced Study Group of the Max Planck Society at CFEL and are using Free Electron Laser radiation for coherent diffractive imaging of biological samples, e.g. viruses.
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