In-cell solid-state NMR as a tool to study proteins in large complexes.
A major limitation of solution NMR is molecular tumbling, which is often too slow for detection. Here we demonstrate that solid-state NMR spectroscopy in combination with flash freezing of cells can be used to detect proteins in the cellular environment and provides information on backbone chemical shifts.
Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt, Germany.
Sina
S
Reckel
Jakob J
JJ
Lopez
Frank
F
Löhr
Clemens
C
Glaubitz
Volker
V
Dötsch
D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology; D006801:Humans; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular; D022061:Tacrolimus Binding Protein 1A / Q000737:chemistry* / Q000378:metabolism; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
D013879:Thioredoxins; D022061:Tacrolimus Binding Protein 1A