Assessing the functionality of a membrane protein in a three-dimensional crystal.
Hexagonal microcrystals of bacteriorhodopsin embedded in a lipidic cubic phase have been investigated by time-resolved FT-IR and resonance Raman spectroscopy. Retinal isomerization, conformational changes in the protein backbone and proton translocation are virtually indistinguishable from those in the native membrane. The protein is thus fully active in three-dimensional crystals.
Institut für Biologische Informationsverarbeitung IBI-2: Structural Biology, Forschungszentrum Jülich GmbH, Jülich, Germany. j.heberle@fz-juelich.de
J
J
Heberle
G
G
Büldt
E
E
Koglin
J P
JP
Rosenbusch
E M
EM
Landau
D000577:Amides / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry*; D003460:Crystallization; D005989:Glycerides / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons; D018717:Purple Membrane / Q000737:chemistry; D012172:Retinaldehyde / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman
D000577:Amides; D005989:Glycerides; D008565:Membrane Proteins; D011522:Protons; D001436:Bacteriorhodopsins; C005953:monoolein; D012172:Retinaldehyde