In situ solid-state NMR spectroscopy of protein in heterogeneous membranes: the baseplate antenna complex of Chlorobaculum tepidum.
A clever combination: an in situ solid-state NMR analysis of CsmA proteins in the heterogeneous environment of the photoreceptor of Chlorobaculum tepidum is reported. Using different combinations of 2D and 3D solid-state NMR spectra, 90 % of the CsmA resonances are assigned and provide on the basis of chemical shift data information about the structure and conformation of CsmA in the CsmA-bacteriochlorophyll a complex.
Department of Chemistry, University of Aarhus, Denmark.
Natalia V
NV
Kulminskaya
Marie Ø
MØ
Pedersen
Morten
M
Bjerring
Jarl
J
Underhaug
Mette
M
Miller
Niels-Ulrik
NU
Frigaard
Jakob T
JT
Nielsen
Niels Chr
NC
Nielsen
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D025541:Bacteriochlorophyll A / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D019414:Chlorobi / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation
D001426:Bacterial Proteins; D025541:Bacteriochlorophyll A; C404706:CsmA protein, Chlorobium tepidum